-% Good, very basic tutorial
-% http://cmtw.harvard.edu/Documentation/TeX/Bibtex/Example.html
-% Really awesome explaination of how BibTeX works
-% http://www.ctan.org/tex-archive/info/bibtex/tamethebeast/
-% More detail on the whole process
-% http://www.andy-roberts.net/misc/latex/latextutorial3.html
-% Entry types reference
-% http://newton.ex.ac.uk/tex/pack/bibtex/btxdoc/node6.html
-% Fields reference
-% http://newton.ex.ac.uk/tex/pack/bibtex/btxdoc/node7.html
-% Entry and field reference, but with little discussion
-% http://en.wikipedia.org/wiki/BibTeX
-% Examples of assorted styles
-% http://www.cs.stir.ac.uk/~kjt/software/latex/showbst.html
-% Assorted BibTeX tools
-% http://liinwww.ira.uka.de/bibliography/Bib.Format.html
-%
-% at some point in your latex document
-% \bibliographystyle{prsty} % Phys. Rev. style
-% other syles include abbrv, alpha, plain, unsrt, ...
-%
-% and in your latex document where you want the bibliography:
-% \bibliography{wtk} % wtk.bib is the name of the database
-%
-% compile (using latex for example) with
-% $ latex example
-% $ bibtex example
-% $ latex example
-% $ latex example
-%
-% See the Natbib package for other citation styles & link formats
-% Customize bibliography with Makebst (`latex makebst`),
-% makes .bst bib-style format files according to your specifications.
-%
-% My key style is '<lowercase-main-author-last-name><two-digit-year>',
-% which I can kindof achieve with
-% $ bibtool -f '%-1n(author)%2d(year)' wtk.bib -o wtk1.bib
-% Except any paper with more than one author has a '.ea' appended to the name
-% and bibtool removes all comments :(.
-
% Define some publisher name shortcuts (useful for consistency)
% Listed in alphebetical order.
@String{AIP = "AIP"}
% Listed in alphebetical order.
@String{ACIEE = "Angewandte Chemie International Edition in English"}
@String{ACIEE = "Angew. Chem. Int. Ed. Engl."}
-@String{ARBC = "Annu. Rev. Biochem."}
-%String{ARBC = "Annual Review of Biochemistry"}
-@String{BCBPRC = "Biochem. Biophys. Res. Commun."}
-%String{BCBPRC = "Biochemical and Biophysical Research Communications"}
+@String{ARBC = "Annual Review of Biochemistry"}
+@String{BCBPRC = "Biochemical and Biophysical Research Communications"}
@String{BPJ = "Biophys. J."}
@String{BIOSENSE = "Biosensors and Bioelectronics"}
@String{EMBO = "EMBO Rep."}
-@String{IJBMM = "Int. J. of Bio. Macromol."}
-%@String{IJBMM = "International Journal of Biological Macromolecules"}
-@String{JCS = "J. Cell Sci."}
-%String{JCS = "Journal of Cell Science"}
+@String{IJBMM = "International Journal of Biological Macromolecules"}
+@String{JCS = "Journal of Cell Science"}
@String{JCP = "The Journal of Chemical Physics"}
-@String{JCPPCB = "J. Chim. Phys."}
-%String{JCPPCB = "Journal de Chimie Physique et de Physico-Chimie Biologique"}
-@String{JMB = "J. Mol. Biol."}
-%String{JMB = "Journal of Molecular Biology"}
+@String{JCPPCB = "Journal de Chimie Physique et de Physico-Chimie Biologique"}
+@String{JMB = "Journal of Molecular Biology"}
@String{JPCM = "Journal of Physics: Condensed Matter"}
@String{LANG = "Langmuir"}
@String{NANOTECH = "Nanotechnology"}
@String{NAT = "Nature"}
-@String{NSB = "Nat. Struct. Biol."}
-%String{NSB = "Nature Structural Biology"}
-@String{NSMB = "Nat. Struct. Mol. Biol."}
-%String{NSMB = "Nature Structural Molecular Biology"}
-@String{NAR = "Nucleic Acids Res."}
-%String{NAR = "Nucleic Acids Research"}
+@String{NSB = "Nature Structural Biology"}
+@String{NSMB = "Nature Structural Molecular Biology"}
+@String{NAR = "Nucleic Acids Research"}
@String{PRL = "Phys. Rev. Lett."}
-@String{PNAS = "PNAS"}
-%String(PNAS = "Proc. Natl. Acad. Sci. USA"}
-%String(PNAS = "Proceedings of the National Academy of Sciences")
-@String{PBPMB = "Prog. Biophys. Mol. Biol."}
-%String{PBPMB = "Progress in Biophysics and Molecular Biology"}
+@String(PNAS = "Proceedings of the National Academy of Sciences USA")
+@String{PBPMB = "Progress in Biophysics and Molecular Biology"}
@String{PS = "Protein Sci."}
@String{PROT = "Proteins"}
@String{RMP = "Rev. Mod. Phys."}
-%String{RSI = "Review of Scientific Instruments"}
-@String{RSI = "Rev. Sci. Instrum."}
+@String{RSI = "Review of Scientific Instruments"}
@String{SCI = "Science"}
@String{STR = "Structure"}
@String{ULTRAMIC = "Ultramicroscopy"}
@String{EChapman = "Chapman, Edwin R."}
@String{JChoy = "Choy, Jason"}
@String{JClarke = "Clarke, Jane"}
-% {\uppercase{d}} is special character for proper "von" parsing.
-% See Tame The BeaST (link at top of file) for details.
@String{EDCola = "{\uppercase{d}}i Cola, Emanuela"}
@String{MConti = "Conti, Matteo"}
@String{DCraig = "Craig, David"}
volume = 100,
number = 18,
pages = "10249--10253",
- keywords = "Protein Folding",
- keywords = "Proteins",
- keywords = "RNA",
- keywords = "Temperature",
- keywords = "Thermodynamics",
+ keywords = "Protein Folding; Proteins; RNA; Temperature; Thermodynamics",
abstract = "By considering temperature effects on the mechanical
unfolding rates of proteins and RNA, whose energy
landscape is rugged, the question posed in the title is
volume = 6,
number = 5,
pages = "482--486",
- keywords = "Models, Molecular",
- keywords = "Protein Binding",
- keywords = "Protein Folding",
- keywords = "Spectrum Analysis",
- keywords = "Thermodynamics",
- keywords = "beta Karyopherins",
- keywords = "ran GTP-Binding Protein",
+ keywords = "Models, Molecular; Protein Binding; Protein Folding; Spectrum Analysis; Thermodynamics; beta Karyopherins; ran GTP-Binding Protein",
abstract = "The energy landscape of proteins is thought to have an
intricate, corrugated structure. Such roughness should
have important consequences on the folding and binding
year = 2000,
month = jun,
day = 20,
- keywords = "Animals",
- keywords = "Humans",
- keywords = "Protein Folding",
- keywords = "Proteins",
- keywords = "Spectrin",
+ keywords = "Animals; Humans; Protein Folding; Proteins; Spectrin",
abstract = "Single-molecule manipulation techniques reveal that
stretching unravels individually folded domains in the
muscle protein titin and the extracellular matrix
year = 2007,
month = dec,
day = 26,
- keywords = "Anisotropy",
- keywords = "Bacterial Proteins",
- keywords = "Biophysics",
- keywords = "Computer Simulation",
- keywords = "Cysteine",
- keywords = "Halorhodospira halophila",
- keywords = "Hydrogen Bonding",
- keywords = "Kinetics",
- keywords = "Luminescent Proteins",
- keywords = "Microscopy, Atomic Force",
- keywords = "Molecular Conformation",
- keywords = "Protein Binding",
- keywords = "Protein Conformation",
- keywords = "Protein Denaturation",
- keywords = "Protein Folding",
- keywords = "Protein Structure, Secondary",
+ keywords = "Anisotropy; Bacterial Proteins; Biophysics; Computer Simulation; Cysteine; Halorhodospira halophila; Hydrogen Bonding; Kinetics; Luminescent Proteins; Microscopy, Atomic Force; Molecular Conformation; Protein Binding; Protein Conformation; Protein Denaturation; Protein Folding; Protein Structure, Secondary",
abstract = "We present a comprehensive study that integrates
experimental and theoretical nonequilibrium techniques
to map energy landscapes along well defined pull-axis
volume = 87,
number = 4,
pages = "2630--2634",
- keywords = "Elasticity",
- keywords = "Enzyme Activation",
- keywords = "Micromanipulation",
- keywords = "Microscopy, Atomic Force",
- keywords = "Models, Chemical",
- keywords = "Models, Molecular",
- keywords = "Multiprotein Complexes",
- keywords = "Nuclear Proteins",
- keywords = "Physical Stimulation",
- keywords = "Protein Binding",
- keywords = "Stress, Mechanical",
- keywords = "Structure-Activity Relationship",
- keywords = "beta Karyopherins",
- keywords = "ran GTP-Binding Protein",
+ keywords = "Elasticity; Enzyme Activation; Micromanipulation; Microscopy, Atomic Force; Models, Chemical; Models, Molecular; Multiprotein Complexes; Nuclear Proteins; Physical Stimulation; Protein Binding; Stress, Mechanical; Structure-Activity Relationship; beta Karyopherins; ran GTP-Binding Protein",
abstract = "The limitations imposed on the analyses of complex
chemical and biological systems by ensemble averaging
can be overcome by single-molecule experiments. Here,
volume = 10,
number = 7,
pages = "553--557",
- keywords = "Guanosine Diphosphate",
- keywords = "Guanosine Triphosphate",
- keywords = "Microscopy, Atomic Force",
- keywords = "Protein Binding",
- keywords = "Protein Conformation",
- keywords = "beta Karyopherins",
- keywords = "ran GTP-Binding Protein",
+ keywords = "Guanosine Diphosphate; Guanosine Triphosphate; Microscopy, Atomic Force; Protein Binding; Protein Conformation; beta Karyopherins; ran GTP-Binding Protein",
abstract = "Several million macromolecules are exchanged each
minute between the nucleus and cytoplasm by
receptor-mediated transport. Most of this traffic is
volume = "90",
number = "4",
pages = "L33--L35",
- keywords = "Models, Molecular",
- keywords = "Protein Folding",
- keywords = "Proteins",
- keywords = "Thermodynamics",
+ keywords = "Models, Molecular; Protein Folding; Proteins; Thermodynamics",
abstract = "The protein folding process is described as diffusion
on a high-dimensional energy landscape. Experimental
data showing details of the underlying energy surface
volume = "92",
number = "6",
pages = "2054--2061",
- keywords = "Computer Simulation",
- keywords = "Models, Chemical",
- keywords = "Models, Molecular",
- keywords = "Models, Statistical",
- keywords = "Monte Carlo Method",
- keywords = "Motion",
- keywords = "Protein Conformation",
- keywords = "Protein Denaturation",
- keywords = "Protein Folding",
- keywords = "Ubiquitin",
+ keywords = "Computer Simulation; Models, Chemical; Models, Molecular; Models, Statistical; Monte Carlo Method; Motion; Protein Conformation; Protein Denaturation; Protein Folding; Ubiquitin",
abstract = "The mechanical unfolding of proteins under a
stretching force has an important role in living
systems and is a logical extension of the more general
volume = 11,
number = 12,
pages = "2759--2765",
- keywords = "Computer Simulation",
- keywords = "Models, Molecular",
- keywords = "Monte Carlo Method",
- keywords = "Protein Folding",
- keywords = "Protein Structure, Tertiary",
- keywords = "Proteins",
+ keywords = "Computer Simulation; Models, Molecular; Monte Carlo Method; Protein Folding; Protein Structure, Tertiary; Proteins",
abstract = "The mechanical resistance of a folded domain in a
polyprotein of five mutant I27 domains (C47S, C63S
I27)(5)is shown to depend on the unfolding history of
volume = "83",
number = "1",
pages = "458--472",
- keywords = "Amino Acid Sequence",
- keywords = "Dose-Response Relationship, Drug",
- keywords = "Kinetics",
- keywords = "Magnetic Resonance Spectroscopy",
- keywords = "Models, Molecular",
- keywords = "Molecular Sequence Data",
- keywords = "Monte Carlo Method",
- keywords = "Muscle Proteins",
- keywords = "Mutation",
- keywords = "Peptide Fragments",
- keywords = "Protein Denaturation",
- keywords = "Protein Folding",
- keywords = "Protein Kinases",
- keywords = "Protein Structure, Secondary",
- keywords = "Protein Structure, Tertiary",
- keywords = "Proteins",
- keywords = "Thermodynamics",
+ keywords = "Amino Acid Sequence; Dose-Response Relationship, Drug; Kinetics; Magnetic Resonance Spectroscopy; Models, Molecular; Molecular Sequence Data; Monte Carlo Method; Muscle Proteins; Mutation; Peptide Fragments; Protein Denaturation; Protein Folding; Protein Kinases; Protein Structure, Secondary; Protein Structure, Tertiary; Proteins; Thermodynamics",
abstract = "It is still unclear whether mechanical unfolding
probes the same pathways as chemical denaturation. To
address this point, we have constructed a concatamer of
volume = "85",
number = "1",
pages = "5--15",
- keywords = "Computer Simulation",
- keywords = "Crystallography",
- keywords = "Energy Transfer",
- keywords = "Kinetics",
- keywords = "Lasers",
- keywords = "Micromanipulation",
- keywords = "Microscopy, Atomic Force",
- keywords = "Models, Molecular",
- keywords = "Molecular Conformation",
- keywords = "Motion",
- keywords = "Muscle Proteins",
- keywords = "Nanotechnology",
- keywords = "Physical Stimulation",
- keywords = "Protein Conformation",
- keywords = "Protein Denaturation",
- keywords = "Protein Folding",
- keywords = "Protein Kinases",
- keywords = "Stress, Mechanical",
+ keywords = "Computer Simulation; Crystallography; Energy Transfer; Kinetics; Lasers; Micromanipulation; Microscopy, Atomic Force; Models, Molecular; Molecular Conformation; Motion; Muscle Proteins; Nanotechnology; Physical Stimulation; Protein Conformation; Protein Denaturation; Protein Folding; Protein Kinases; Stress, Mechanical",
abstract = "Mechanical forces exerted by laser tweezers or atomic
force microscopes can be used to drive rare transitions
in single molecules, such as unfolding of a protein or
volume = "6",
number = "1",
pages = "46--51",
- keywords = "Animals",
- keywords = "Contractile Proteins",
- keywords = "Dictyostelium",
- keywords = "Immunoglobulins",
- keywords = "Kinetics",
- keywords = "Microfilament Proteins",
- keywords = "Models, Molecular",
- keywords = "Protein Folding",
- keywords = "Protein Structure, Tertiary",
+ keywords = "Animals; Contractile Proteins; Dictyostelium; Immunoglobulins; Kinetics; Microfilament Proteins; Models, Molecular; Protein Folding; Protein Structure, Tertiary",
abstract = "The F-actin crosslinker filamin from Dictyostelium
discoideum (ddFLN) has a rod domain consisting of six
structurally similar immunoglobulin domains. When
volume = "76",
number = "5",
pages = "2439--2447",
- keywords = "Animals",
- keywords = "Biophysics",
- keywords = "Biopolymers",
- keywords = "Microscopy, Atomic Force",
- keywords = "Models, Chemical",
- keywords = "Muscle Proteins",
- keywords = "Protein Folding",
- keywords = "Protein Kinases",
- keywords = "Stochastic Processes",
- keywords = "Stress, Mechanical",
- keywords = "Thermodynamics",
+ keywords = "Animals; Biophysics; Biopolymers; Microscopy, Atomic Force; Models, Chemical; Muscle Proteins; Protein Folding; Protein Kinases; Stochastic Processes; Stress, Mechanical; Thermodynamics",
abstract = "Bond dissociation under steadily rising force occurs
most frequently at a time governed by the rate of
loading (Evans and Ritchie, 1997 Biophys. J.
volume = "72",
number = "4",
pages = "1541--1555",
- keywords = "Avidin",
- keywords = "Biotin",
- keywords = "Chemistry, Physical",
- keywords = "Computer Simulation",
- keywords = "Mathematics",
- keywords = "Monte Carlo Method",
- keywords = "Protein Binding",
+ keywords = "Avidin; Biotin; Chemistry, Physical; Computer Simulation; Mathematics; Monte Carlo Method; Protein Binding",
abstract = "In biology, molecular linkages at, within, and beneath
cell interfaces arise mainly from weak noncovalent
interactions. These bonds will fail under any level of
volume = "1",
number = "6",
pages = "441--450",
- keywords = "Animals",
- keywords = "Cytochrome c Group",
- keywords = "Humans",
- keywords = "Infant",
- keywords = "Protein Folding",
+ keywords = "Animals; Cytochrome c Group; Humans; Infant; Protein Folding",
abstract = "BACKGROUND: Energy landscape theory predicts that the
folding funnel for a small fast-folding alpha-helical
protein will have a transition state half-way to the
volume = {104},
number = {15},
pages = {5860--5868},
-keywords = {PROTEINS; FOLDS; DIFFUSION; MONTE CARLO METHOD; SIMULATION; FREE ENERGY},
+ keywords = {PROTEINS; FOLDS; DIFFUSION; MONTE CARLO METHOD; SIMULATION; FREE ENERGY},
abstract = {The quantitative description
of model protein folding kinetics using a diffusive
collective reaction coordinate is examined.
volume = 11,
number = 1,
pages = "81--85",
- keywords = "Actins",
- keywords = "Animals",
- keywords = "Contractile Proteins",
- keywords = "Cross-Linking Reagents",
- keywords = "Dictyostelium",
- keywords = "Dimerization",
- keywords = "Microfilament Proteins",
- keywords = "Microscopy, Atomic Force",
- keywords = "Mutagenesis, Site-Directed",
- keywords = "Protein Denaturation",
- keywords = "Protein Folding",
- keywords = "Protein Structure, Tertiary",
- keywords = "Protozoan Proteins",
+ keywords = "Actins; Animals; Contractile Proteins; Cross-Linking Reagents; Dictyostelium; Dimerization; Microfilament Proteins; Microscopy, Atomic Force; Mutagenesis, Site-Directed; Protein Denaturation; Protein Folding; Protein Structure, Tertiary; Protozoan Proteins",
abstract = "Many F-actin crosslinking proteins consist of two
actin-binding domains separated by a rod domain that
can vary considerably in length and structure. In this
volume = "200",
number = "4342",
pages = "618--627",
- keywords = "Antigen-Antibody Reactions",
- keywords = "Cell Adhesion",
- keywords = "Cell Membrane",
- keywords = "Chemistry, Physical",
- keywords = "Electrophysiology",
- keywords = "Enzymes",
- keywords = "Glycoproteins",
- keywords = "Kinetics",
- keywords = "Ligands",
- keywords = "Membrane Proteins",
- keywords = "Models, Biological",
- keywords = "Receptors, Drug",
+ keywords = "Antigen-Antibody Reactions; Cell Adhesion; Cell Membrane; Chemistry, Physical; Electrophysiology; Enzymes; Glycoproteins; Kinetics; Ligands; Membrane Proteins; Models, Biological; Receptors, Drug",
abstract = "A theoretical framework is proposed for the analysis
of adhesion between cells or of cells to surfaces when
the adhesion is mediated by reversible bonds between
volume = "101",
number = "39",
pages = "14102--14107",
- keywords = "Animals",
- keywords = "Ankyrin Repeat",
- keywords = "Circular Dichroism",
- keywords = "Drosophila Proteins",
- keywords = "Drosophila melanogaster",
- keywords = "Gene Deletion",
- keywords = "Models, Chemical",
- keywords = "Models, Molecular",
- keywords = "Protein Denaturation",
- keywords = "Protein Folding",
- keywords = "Protein Structure, Tertiary",
- keywords = "Spectrometry, Fluorescence",
- keywords = "Thermodynamics",
- keywords = "Urea",
+ keywords = "Animals; Ankyrin Repeat; Circular Dichroism; Drosophila Proteins; Drosophila melanogaster; Gene Deletion; Models, Chemical; Models, Molecular; Protein Denaturation; Protein Folding; Protein Structure, Tertiary; Spectrometry, Fluorescence; Thermodynamics; Urea",
abstract = "Energy landscapes have been used to conceptually
describe and model protein folding but have been
difficult to measure experimentally, in large part
volume = "21",
number = "3",
pages = "167--195",
- keywords = "Amino Acid Sequence",
- keywords = "Chemistry, Physical",
- keywords = "Computer Simulation",
- keywords = "Data Interpretation, Statistical",
- keywords = "Kinetics",
- keywords = "Models, Chemical",
- keywords = "Molecular Sequence Data",
- keywords = "Protein Biosynthesis",
- keywords = "Protein Conformation",
- keywords = "Protein Folding",
- keywords = "Proteins",
- keywords = "Thermodynamics",
+ keywords = "Amino Acid Sequence; Chemistry, Physical; Computer Simulation; Data Interpretation, Statistical; Kinetics; Models, Chemical; Molecular Sequence Data; Protein Biosynthesis; Protein Conformation; Protein Folding; Proteins; Thermodynamics",
abstract = "The understanding, and even the description of protein
folding is impeded by the complexity of the process.
Much of this complexity can be described and understood
volume = "84",
number = "21",
pages = "7524--7528",
- keywords = "Kinetics",
- keywords = "Mathematics",
- keywords = "Models, Theoretical",
- keywords = "Protein Conformation",
- keywords = "Proteins",
- keywords = "Stochastic Processes",
+ keywords = "Kinetics; Mathematics; Models, Theoretical; Protein Conformation; Proteins; Stochastic Processes",
abstract = "The theory of spin glasses was used to study a simple
model of protein folding. The phase diagram of the
model was calculated, and the results of dynamics
volume = 265,
number = 5178,
pages = "1599--1600",
- keywords = "Bacteriophage lambda",
- keywords = "DNA, Viral",
- keywords = "Least-Squares Analysis",
- keywords = "Thermodynamics",
+ keywords = "Bacteriophage lambda; DNA, Viral; Least-Squares Analysis; Thermodynamics",
ISSN = "0036-8075",
doi = "10.1126/science.8079175",
url = "http://www.sciencemag.org/cgi/content/abstract/265/5178/1599",
volume = "92",
number = "12",
pages = "4188--4195",
- keywords = "Computer Simulation",
- keywords = "DNA",
- keywords = "Elasticity",
- keywords = "Mechanics",
- keywords = "Micromanipulation",
- keywords = "Microscopy, Atomic Force",
- keywords = "Models, Chemical",
- keywords = "Models, Molecular",
- keywords = "Nanostructures",
- keywords = "Nucleic Acid Conformation",
- keywords = "Porosity",
- keywords = "Stress, Mechanical",
+ keywords = "Computer Simulation;DNA;Elasticity;Mechanics;Micromanipulation;Microscopy, Atomic Force;Models, Chemical;Models, Molecular;Nanostructures;Nucleic Acid Conformation;Porosity;Stress, Mechanical",
abstract = "Single-molecule force experiments provide powerful new
tools to explore biomolecular interactions. Here, we
describe a systematic procedure for extracting kinetic
volume = "96",
number = "10",
pages = "108101",
- keywords = "Biophysics",
- keywords = "Computer Simulation",
- keywords = "Data Interpretation, Statistical",
- keywords = "Kinetics",
- keywords = "Micromanipulation",
- keywords = "Models, Chemical",
- keywords = "Models, Molecular",
- keywords = "Molecular Conformation",
- keywords = "Muscle Proteins",
- keywords = "Nucleic Acid Conformation",
- keywords = "Protein Binding",
- keywords = "Protein Denaturation",
- keywords = "Protein Folding",
- keywords = "Protein Kinases",
- keywords = "RNA",
- keywords = "Stress, Mechanical",
- keywords = "Thermodynamics",
- keywords = "Time Factors",
+ keywords = "Biophysics;Computer Simulation;Data Interpretation, Statistical;Kinetics;Micromanipulation;Models, Chemical;Models, Molecular;Molecular Conformation;Muscle Proteins;Nucleic Acid Conformation;Protein Binding;Protein Denaturation;Protein Folding;Protein Kinases;RNA;Stress, Mechanical;Thermodynamics;Time Factors",
abstract = "We present a unified framework for extracting kinetic
information from single-molecule pulling experiments at
constant force or constant pulling speed. Our procedure
volume = "213",
number = "4",
pages = "527--545",
- keywords = "Adult",
- keywords = "Aged",
- keywords = "Aging",
- keywords = "Animals",
- keywords = "Humans",
- keywords = "Longevity",
- keywords = "Middle Aged",
- keywords = "Models, Biological",
- keywords = "Survival Rate",
- keywords = "Systems Theory",
+ keywords = "Adult;Aged;Aging;Animals;Humans;Longevity;Middle Aged;Models, Biological;Survival Rate;Systems Theory",
abstract = "Reliability theory is a general theory about systems
failure. It allows researchers to predict the
age-related failure kinetics for a system of given
volume = "34",
number = "1",
pages = "1--15",
- keywords = "Aging",
- keywords = "Biometry",
- keywords = "History, 19th Century",
- keywords = "History, 20th Century",
- keywords = "Humans",
- keywords = "Life Tables",
- keywords = "Mortality",
- keywords = "Sexual Maturation",
+ keywords = "Aging;Biometry;History, 19th Century;History, 20th Century;Humans;Life Tables;Mortality;Sexual Maturation",
abstract = "In 1825 British actuary Benjamin Gompertz made a
simple but important observation that a law of
geometrical progression pervades large portions of
volume = 69,
number = "1--2",
pages = "1--31",
- keywords = "Adolescent",
- keywords = "Adult",
- keywords = "Aged",
- keywords = "Aged, 80 and over",
- keywords = "Aging",
- keywords = "Biometry",
- keywords = "Child",
- keywords = "Child, Preschool",
- keywords = "Data Interpretation, Statistical",
- keywords = "Female",
- keywords = "Humans",
- keywords = "Infant",
- keywords = "Infant, Newborn",
- keywords = "Longitudinal Studies",
- keywords = "Male",
- keywords = "Middle Aged",
- keywords = "Models, Biological",
- keywords = "Models, Statistical",
- keywords = "Mortality",
+ keywords = "Adolescent;Adult;Aged;Aged, 80 and over;Aging;Biometry;Child;Child, Preschool;Data Interpretation, Statistical;Female;Humans;Infant;Infant, Newborn;Longitudinal Studies;Male;Middle Aged;Models, Biological;Models, Statistical;Mortality",
abstract = "The Gompertz and Weibull functions are compared with
respect to goodness-of-fit to human mortality
distributions; ability to describe mortality curve
volume = "3",
number = "3",
pages = "255--261",
- keywords = "Ligands",
- keywords = "Microscopy, Atomic Force",
- keywords = "Polysaccharides",
- keywords = "Protein Denaturation",
- keywords = "Proteins",
+ keywords = "Ligands;Microscopy, Atomic Force;Polysaccharides;Protein Denaturation;Proteins",
abstract = "Many processes in the body are effected and regulated
by highly specialized protein molecules: These
molecules certainly deserve the name ``biochemical
volume = "112",
number = "1-2",
pages = "13--23",
- keywords = "Binding Sites",
- keywords = "Computer Simulation",
- keywords = "DNA",
- keywords = "DNA-Binding Proteins",
- keywords = "Elasticity",
- keywords = "Ligands",
- keywords = "Macromolecular Substances",
- keywords = "Micromanipulation",
- keywords = "Microscopy, Atomic Force",
- keywords = "Models, Chemical",
- keywords = "Molecular Biology",
- keywords = "Nucleic Acid Conformation",
- keywords = "Physical Stimulation",
- keywords = "Protein Binding",
- keywords = "Protein Conformation",
- keywords = "Stress, Mechanical",
+ keywords = "Binding Sites;Computer Simulation;DNA;DNA-Binding Proteins;Elasticity;Ligands;Macromolecular Substances;Micromanipulation;Microscopy, Atomic Force;Models, Chemical;Molecular Biology;Nucleic Acid Conformation;Physical Stimulation;Protein Binding;Protein Conformation;Stress, Mechanical",
abstract = "The forced rupture of single chemical bonds in
biomolecular compounds (e.g. ligand-receptor systems)
as observed in dynamic force spectroscopy experiments
volume = "90",
number = "11",
pages = "3851--3864",
- keywords = "Biomechanics",
- keywords = "Microscopy, Atomic Force",
- keywords = "Models, Molecular",
- keywords = "Statistical Distributions",
- keywords = "Thermodynamics",
+ keywords= "Biomechanics;Microscopy, Atomic Force;Models, Molecular;Statistical Distributions;Thermodynamics",
abstract = "We show that the standard theoretical framework in
single-molecule force spectroscopy has to be extended
to consistently describe the experimental findings. The
volume = {72},
number = {8},
pages = {4350--4357},
-keywords = {DIFFUSION; CHEMICAL REACTIONS; CHEMICAL REACTION KINETICS; PROBABILITY; DIFFERENTIAL EQUATIONS},
+ keywords = {DIFFUSION; CHEMICAL REACTIONS; CHEMICAL REACTION KINETICS; PROBABILITY; DIFFERENTIAL EQUATIONS},
url = {http://link.aip.org/link/?JCP/72/4350/1},
doi = {10.1063/1.439715}
}
volume = "100",
number = "20",
pages = "11378--11381",
- keywords = "Spectrum Analysis",
- keywords = "Temperature",
+ keywords = "Spectrum Analysis;Temperature",
abstract = "Dynamic force spectroscopy of single molecules is
described by a model that predicts a distribution of
rupture forces, the corresponding mean rupture force,
volume = "73",
number = "3",
pages = "1281--1287",
- keywords = "Binding Sites",
- keywords = "Biopolymers",
- keywords = "Kinetics",
- keywords = "Ligands",
- keywords = "Microscopy, Atomic Force",
- keywords = "Models, Chemical",
- keywords = "Molecular Conformation",
- keywords = "Protein Conformation",
- keywords = "Proteins",
- keywords = "Reproducibility of Results",
- keywords = "Stochastic Processes",
- keywords = "Thermodynamics",
+ keywords = "Binding Sites;Biopolymers;Kinetics;Ligands;Microscopy, Atomic Force;Models, Chemical;Molecular Conformation;Protein Conformation;Proteins;Reproducibility of Results;Stochastic Processes;Thermodynamics",
abstract = "One-dimensional stochastic models demonstrate that
molecular dynamics simulations of a few nanoseconds can
be used to reconstruct the essential features of the
volume = "72",
number = "4",
pages = "1568--1581",
- keywords = "Avidin",
- keywords = "Binding Sites",
- keywords = "Biotin",
- keywords = "Computer Simulation",
- keywords = "Hydrogen Bonding",
- keywords = "Mathematics",
- keywords = "Microscopy, Atomic Force",
- keywords = "Microspheres",
- keywords = "Models, Molecular",
- keywords = "Molecular Structure",
- keywords = "Protein Binding",
- keywords = "Protein Conformation",
- keywords = "Protein Folding",
- keywords = "Sepharose",
+ keywords = "Avidin;Binding Sites;Biotin;Computer Simulation;Hydrogen Bonding;Mathematics;Microscopy, Atomic Force;Microspheres;Models, Molecular;Molecular Structure;Protein Binding;Protein Conformation;Protein Folding;Sepharose",
abstract = "We report molecular dynamics simulations that induce,
over periods of 40-500 ps, the unbinding of biotin from
avidin by means of external harmonic forces with force
volume = 402,
number = 6757,
pages = "100--103",
- keywords = "Biomechanics",
- keywords = "Computer Simulation",
- keywords = "Humans",
- keywords = "Hydrogen Bonding",
- keywords = "Microscopy, Atomic Force",
- keywords = "Models, Molecular",
- keywords = "Muscle Proteins",
- keywords = "Myocardium",
- keywords = "Protein Folding",
- keywords = "Protein Kinases",
- keywords = "Recombinant Proteins",
+ keywords = "Biomechanics;Computer Simulation;Humans;Hydrogen Bonding;Microscopy, Atomic Force;Models, Molecular;Muscle Proteins;Myocardium;Protein Folding;Protein Kinases;Recombinant Proteins",
abstract = "The modular protein titin, which is responsible for
the passive elasticity of muscle, is subjected to
stretching forces. Previous work on the experimental
volume = "35",
number = "4",
pages = "527--531",
- keywords = "Biomechanics",
- keywords = "Cross-Linking Reagents",
- keywords = "Elasticity",
- keywords = "Extracellular Matrix",
- keywords = "Humans",
- keywords = "Hyaluronic Acid",
- keywords = "Lasers",
- keywords = "Microspheres",
- keywords = "Nanotechnology",
+ keywords = "Biomechanics;Cross-Linking Reagents;Elasticity;Extracellular Matrix;Humans;Hyaluronic Acid;Lasers;Microspheres;Nanotechnology",
abstract = "Hyaluronan (HA) is a major component of the
extracellular matrix. It plays an important role in the
mechanical functions of the extracellular matrix and
volume = "33",
number = "9-10",
pages = "553--558",
- keywords = "Animals",
- keywords = "Culture Media",
- keywords = "Humans",
- keywords = "Hyaluronic Acid",
- keywords = "Hyaluronoglucosaminidase",
- keywords = "Mice",
- keywords = "Mice, Nude",
- keywords = "Neoplasm Metastasis",
- keywords = "Neoplasm Transplantation",
- keywords = "Neoplasms, Experimental",
- keywords = "Tumor Cells, Cultured",
+ keywords = "Animals;Culture Media;Humans;Hyaluronic Acid;Hyaluronoglucosaminidase;Mice;Mice, Nude;Neoplasm Metastasis;Neoplasm Transplantation;Neoplasms, Experimental;Tumor Cells, Cultured",
abstract = "To approach the question of hyaluronan catabolism in
tumours, we have selected the cancer cell line H460M, a
highly metastatic cell line in the nude mouse. H460M
volume = 75,
number = 2,
pages = "662--671",
- keywords = "Amino Acid Sequence",
- keywords = "Animals",
- keywords = "Computer Simulation",
- keywords = "Glutamic Acid",
- keywords = "Immunoglobulins",
- keywords = "Lysine",
- keywords = "Macromolecular Substances",
- keywords = "Models, Molecular",
- keywords = "Molecular Sequence Data",
- keywords = "Muscle Proteins",
- keywords = "Myocardium",
- keywords = "Proline",
- keywords = "Protein Denaturation",
- keywords = "Protein Folding",
- keywords = "Protein Kinases",
- keywords = "Protein Structure, Secondary",
- keywords = "Sequence Alignment",
- keywords = "Sequence Homology, Amino Acid",
- keywords = "Valine",
+ keywords = "Amino Acid Sequence;Animals;Computer Simulation;Glutamic Acid;Immunoglobulins;Lysine;Macromolecular Substances;Models, Molecular;Molecular Sequence Data;Muscle Proteins;Myocardium;Proline;Protein Denaturation;Protein Folding;Protein Kinases;Protein Structure, Secondary;Sequence Alignment;Sequence Homology, Amino Acid;Valine",
abstract = "Titin, a 1-microm-long protein found in striated
muscle myofibrils, possesses unique elastic and
extensibility properties in its I-band region, which is
volume = 35,
number = 4,
pages = "453--463",
- keywords = "Computer Simulation",
- keywords = "Fibronectins",
- keywords = "Hydrogen Bonding",
- keywords = "Microscopy, Atomic Force",
- keywords = "Models, Molecular",
- keywords = "Protein Denaturation",
+ keywords = "Computer Simulation;Fibronectins;Hydrogen Bonding;Microscopy, Atomic Force;Models, Molecular;Protein Denaturation",
abstract = "Steered molecular dynamics (SMD), a computer
simulation method for studying force-induced reactions
in biopolymers, has been applied to investigate the
volume = "96",
number = "4",
pages = "1351--1356",
- keywords = "Amino Acid Sequence",
- keywords = "Binding Sites",
- keywords = "Computer Simulation",
- keywords = "Crystallography, X-Ray",
- keywords = "Disulfides",
- keywords = "Fibronectins",
- keywords = "Hydrogen Bonding",
- keywords = "Integrins",
- keywords = "Models, Molecular",
- keywords = "Oligopeptides",
- keywords = "Protein Conformation",
- keywords = "Protein Denaturation",
- keywords = "Protein Folding",
- keywords = "Protein Structure, Secondary",
- keywords = "Protein Structure, Tertiary",
- keywords = "Software",
- keywords = "Tensile Strength",
+ keywords = "Amino Acid Sequence;Binding Sites;Computer Simulation;Crystallography, X-Ray;Disulfides;Fibronectins;Hydrogen Bonding;Integrins;Models, Molecular;Oligopeptides;Protein Conformation;Protein Denaturation;Protein Folding;Protein Structure, Secondary;Protein Structure, Tertiary;Software;Tensile Strength",
abstract = "The 10th type III module of fibronectin possesses a
beta-sandwich structure consisting of seven
beta-strands (A-G) that are arranged in two
volume = "96",
number = "5",
pages = "2031--2035",
- keywords = "Amino Acid Sequence",
- keywords = "Drug Stability",
- keywords = "Kinetics",
- keywords = "Models, Theoretical",
- keywords = "Molecular Sequence Data",
- keywords = "Peptides",
- keywords = "Protein Denaturation",
- keywords = "Protein Folding",
+ keywords = "Amino Acid Sequence;Drug Stability;Kinetics;Models, Theoretical;Molecular Sequence Data;Peptides;Protein Denaturation;Protein Folding",
abstract = "A new class of experiments that probe folding of
individual protein domains uses mechanical stretching
to cause the transition. We show how stretching forces
volume = "288",
number = "3",
pages = "441--459",
- keywords = "Dimerization",
- keywords = "Fibronectins",
- keywords = "Humans",
- keywords = "Hydrogen Bonding",
- keywords = "Microscopy, Atomic Force",
- keywords = "Protein Denaturation",
- keywords = "Protein Folding",
+ keywords = "Dimerization;Fibronectins;Humans;Hydrogen Bonding;Microscopy, Atomic Force;Protein Denaturation;Protein Folding",
abstract = "Titin, an important constituent of vertebrate muscles,
is a protein of the order of a micrometer in length in
the folded state. Atomic force microscopy and laser
year = "2000",
volume = "481",
pages = "143--60",
- keywords = "Amino Acid Sequence",
- keywords = "Animals",
- keywords = "Computer Simulation",
- keywords = "Elasticity",
- keywords = "Fibronectins",
- keywords = "Humans",
- keywords = "Hydrogen Bonding",
- keywords = "Immunoglobulins",
- keywords = "Models, Molecular",
- keywords = "Muscle Proteins",
- keywords = "Muscle, Skeletal",
- keywords = "Myofibrils",
- keywords = "Protein Conformation",
- keywords = "Protein Denaturation",
- keywords = "Protein Kinases",
- keywords = "Software",
+ keywords = "Amino Acid Sequence;Animals;Computer Simulation;Elasticity;Fibronectins;Humans;Hydrogen Bonding;Immunoglobulins;Models, Molecular;Muscle Proteins;Muscle, Skeletal;Myofibrils;Protein Conformation;Protein Denaturation;Protein Kinases;Software",
abstract = "Titin, a 1 micron long protein found in striated
muscle myofibrils, possesses unique elastic and
extensibility properties, and is largely composed of a
volume = "79",
number = "1",
pages = "51--65",
- keywords = "Amino Acid Sequence",
- keywords = "Computer Simulation",
- keywords = "Double Bind Interaction",
- keywords = "Hydrogen Bonding",
- keywords = "Immunoglobulins",
- keywords = "Microscopy, Atomic Force",
- keywords = "Models, Chemical",
- keywords = "Models, Molecular",
- keywords = "Molecular Sequence Data",
- keywords = "Muscle Proteins",
- keywords = "Protein Folding",
- keywords = "Protein Kinases",
- keywords = "Protein Structure, Tertiary",
- keywords = "Stress, Mechanical",
- keywords = "Water",
+ keywords = "Amino Acid Sequence;Computer Simulation;Double Bind Interaction;Hydrogen Bonding;Immunoglobulins;Microscopy, Atomic Force;Models, Chemical;Models, Molecular;Molecular Sequence Data;Muscle Proteins;Protein Folding;Protein Kinases;Protein Structure, Tertiary;Stress, Mechanical;Water",
abstract = "Steered molecular dynamics simulation of force-induced
titin immunoglobulin domain I27 unfolding led to the
discovery of a significant potential energy barrier at
volume = "63",
number = "2 Pt 1",
pages = "021906",
- keywords = "Biophysics",
- keywords = "Macromolecular Substances",
- keywords = "Microscopy, Atomic Force",
- keywords = "Models, Statistical",
- keywords = "Models, Theoretical",
- keywords = "Statistics as Topic",
+ keywords = "Biophysics;Macromolecular Substances;Microscopy, Atomic Force;Models, Statistical;Models, Theoretical;Statistics as Topic",
abstract = "We formulate the proper statistical mechanics to
describe the stretching of a macromolecule under a
force provided by the cantilever of an atomic force
volume = 276,
number = 5315,
pages = "1112--1116",
- keywords = "Amino Acid Sequence",
- keywords = "Elasticity",
- keywords = "Entropy",
- keywords = "Immunoglobulins",
- keywords = "Lasers",
- keywords = "Models, Chemical",
- keywords = "Muscle Contraction",
- keywords = "Muscle Proteins",
- keywords = "Muscle Relaxation",
- keywords = "Muscle, Skeletal",
- keywords = "Protein Denaturation",
- keywords = "Protein Folding",
- keywords = "Protein Kinases",
- keywords = "Stress, Mechanical",
+ keywords = "Amino Acid Sequence;Elasticity;Entropy;Immunoglobulins;Lasers;Models, Chemical;Muscle Contraction;Muscle Proteins;Muscle Relaxation;Muscle, Skeletal;Protein Denaturation;Protein Folding;Protein Kinases;Stress, Mechanical",
abstract = "Titin, a giant filamentous polypeptide, is believed to
play a fundamental role in maintaining sarcomeric
structural integrity and developing what is known as
month = jun,
volume = "111 (Pt 11)",
pages = "1567--1574",
- keywords = "Animals",
- keywords = "Elasticity",
- keywords = "Immunoglobulins",
- keywords = "Male",
- keywords = "Muscle Proteins",
- keywords = "Muscle, Skeletal",
- keywords = "Protein Kinases",
- keywords = "Rats",
- keywords = "Rats, Wistar",
- keywords = "Structure-Activity Relationship",
+ keywords = "Animals;Elasticity;Immunoglobulins;Male;Muscle Proteins;Muscle, Skeletal;Protein Kinases;Rats;Rats, Wistar;Structure-Activity Relationship",
abstract = "The poly-immunoglobulin domain region of titin,
located within the elastic section of this giant muscle
protein, determines the extensibility of relaxed
volume = "95",
number = "14",
pages = "8052--8057",
- keywords = "Animals",
- keywords = "Elasticity",
- keywords = "Fluorescent Antibody Technique",
- keywords = "Male",
- keywords = "Microscopy, Immunoelectron",
- keywords = "Muscle Proteins",
- keywords = "Muscle, Skeletal",
- keywords = "Protein Kinases",
- keywords = "Rats",
- keywords = "Rats, Wistar",
- keywords = "Stress, Mechanical",
+ keywords = "Animals;Elasticity;Fluorescent Antibody Technique;Male;Microscopy, Immunoelectron;Muscle Proteins;Muscle, Skeletal;Protein Kinases;Rats;Rats, Wistar;Stress, Mechanical",
abstract = "A unique sequence within the giant titin molecule, the
PEVK domain, has been suggested to greatly contribute
to passive force development of relaxed skeletal muscle
volume = 271,
number = 5250,
pages = "795--799",
- keywords = "Base Composition",
- keywords = "Chemistry, Physical",
- keywords = "DNA",
- keywords = "DNA, Single-Stranded",
- keywords = "Elasticity",
- keywords = "Nucleic Acid Conformation",
- keywords = "Osmolar Concentration",
- keywords = "Thermodynamics",
+ keywords = "Base Composition;Chemistry, Physical;DNA;DNA, Single-Stranded;Elasticity;Nucleic Acid Conformation;Osmolar Concentration;Thermodynamics",
abstract = "Single molecules of double-stranded DNA (dsDNA) were
stretched with force-measuring laser tweezers. Under a
longitudinal stress of approximately 65 piconewtons
volume = "96",
number = "11",
pages = "6166--6170",
- keywords = "Amino Acid Sequence",
- keywords = "Kinetics",
- keywords = "Models, Chemical",
- keywords = "Protein Denaturation",
- keywords = "Protein Folding",
- keywords = "Proteins",
- keywords = "Thermodynamics",
- keywords = "Time Factors",
+ keywords = "Amino Acid Sequence;Kinetics;Models, Chemical;Protein Denaturation;Protein Folding;Proteins;Thermodynamics;Time Factors",
abstract = "Single-molecule force spectroscopy reveals unfolding
of domains in titin on stretching. We provide a
theoretical framework for these experiments by
volume = "2",
number = "1",
pages = "53--61",
- keywords = "Animals",
- keywords = "Data Collection",
- keywords = "Humans",
- keywords = "Microscopy, Atomic Force",
- keywords = "Microscopy, Fluorescence",
- keywords = "Molecular Biology",
+ keywords = "Animals;Data Collection;Humans;Microscopy, Atomic Force;Microscopy, Fluorescence;Molecular Biology",
abstract = "Single-molecule methods have revolutionized scientific
research by rendering the investigation of
once-inaccessible biological processes amenable to
volume = "85",
number = "5",
pages = "3286--3293",
- keywords = "Circular Dichroism",
- keywords = "Elasticity",
- keywords = "Heat",
- keywords = "Microscopy, Atomic Force",
- keywords = "Physical Stimulation",
- keywords = "Protein Conformation",
- keywords = "Protein Denaturation",
- keywords = "Protein Folding",
- keywords = "Protein Structure, Tertiary",
- keywords = "Spectrin",
- keywords = "Stress, Mechanical",
- keywords = "Temperature",
+ keywords = "Circular Dichroism;Elasticity;Heat;Microscopy, Atomic Force;Physical Stimulation;Protein Conformation;Protein Denaturation;Protein Folding;Protein Structure, Tertiary;Spectrin;Stress, Mechanical;Temperature",
abstract = "Pathways of unfolding a protein depend in principle on
the perturbation-whether it is temperature, denaturant,
or even forced extension. Widely-shared, helical-bundle
volume = 258,
number = 5085,
pages = "1122--1126",
- keywords = "Chemistry, Physical",
- keywords = "Cisplatin",
- keywords = "DNA",
- keywords = "Elasticity",
- keywords = "Ethidium",
- keywords = "Glass",
- keywords = "Indoles",
- keywords = "Intercalating Agents",
- keywords = "Magnetics",
- keywords = "Mathematics",
- keywords = "Microspheres",
+ keywords = "Chemistry, Physical;Cisplatin;DNA;Elasticity;Ethidium;Glass;Indoles;Intercalating Agents;Magnetics;Mathematics;Microspheres",
abstract = "Single DNA molecules were chemically attached by one
end to a glass surface and by their other end to a
magnetic bead. Equilibrium positions of the beads were
volume = 271,
number = 5257,
pages = "1835--1837",
- keywords = "Bacteriophage lambda",
- keywords = "DNA, Superhelical",
- keywords = "DNA, Viral",
- keywords = "Elasticity",
- keywords = "Magnetics",
- keywords = "Nucleic Acid Conformation",
- keywords = "Temperature",
+ keywords = "Bacteriophage lambda;DNA, Superhelical;DNA, Viral;Elasticity;Magnetics;Nucleic Acid Conformation;Temperature",
abstract = "Single linear DNA molecules were bound at multiple
sites at one extremity to a treated glass cover slip
and at the other to a magnetic bead. The DNA was
volume = "13",
number = "3",
pages = "266--274",
- keywords = "DNA",
- keywords = "DNA-Binding Proteins",
- keywords = "Isomerases",
- keywords = "Micromanipulation",
- keywords = "Microscopy, Atomic Force",
- keywords = "Nucleic Acid Conformation",
- keywords = "Nucleotidyltransferases",
+ keywords = "DNA;DNA-Binding Proteins;Isomerases;Micromanipulation;Microscopy, Atomic Force;Nucleic Acid Conformation;Nucleotidyltransferases",
abstract = "When interacting with a single stretched DNA, many
proteins modify its end-to-end distance. This distance
can be monitored in real time using various
volume = 6,
number = 4,
pages = "346--349",
- keywords = "Bacteriophage lambda",
- keywords = "Base Pairing",
- keywords = "DNA",
- keywords = "DNA, Single-Stranded",
- keywords = "DNA, Viral",
- keywords = "Gold",
- keywords = "Mechanics",
- keywords = "Microscopy, Atomic Force",
- keywords = "Nucleotides",
- keywords = "Spectrum Analysis",
- keywords = "Thermodynamics",
+ keywords = "Bacteriophage lambda;Base Pairing;DNA;DNA, Single-Stranded;DNA, Viral;Gold;Mechanics;Microscopy, Atomic Force;Nucleotides;Spectrum Analysis;Thermodynamics",
abstract = "Atomic force microscope-based single-molecule force
spectroscopy was employed to measure sequence-dependent
mechanical properties of DNA by stretching individual
volume = 87,
number = 6,
pages = "3995--4006",
- keywords = "Computer Simulation",
- keywords = "Elasticity",
- keywords = "Mechanics",
- keywords = "Micromanipulation",
- keywords = "Microscopy, Atomic Force",
- keywords = "Models, Chemical",
- keywords = "Models, Molecular",
- keywords = "Protein Conformation",
- keywords = "Protein Denaturation",
- keywords = "Protein Folding",
- keywords = "Stress, Mechanical",
- keywords = "Structure-Activity Relationship",
- keywords = "Ubiquitin",
+ keywords = "Computer Simulation;Elasticity;Mechanics;Micromanipulation;Microscopy, Atomic Force;Models, Chemical;Models, Molecular;Protein Conformation;Protein Denaturation;Protein Folding;Stress, Mechanical;Structure-Activity Relationship;Ubiquitin",
abstract = "Single-molecule manipulation techniques have enabled
the characterization of the unfolding and refolding
process of individual protein molecules, using
volume = "10",
number = "9",
pages = "738--743",
- keywords = "Humans",
- keywords = "Hydrogen Bonding",
- keywords = "Kinetics",
- keywords = "Lysine",
- keywords = "Microscopy, Atomic Force",
- keywords = "Models, Molecular",
- keywords = "Polyubiquitin",
- keywords = "Protein Binding",
- keywords = "Protein Folding",
- keywords = "Protein Structure, Tertiary",
- keywords = "Ubiquitin",
+ keywords = "Humans;Hydrogen Bonding;Kinetics;Lysine;Microscopy, Atomic Force;Models, Molecular;Polyubiquitin;Protein Binding;Protein Folding;Protein Structure, Tertiary;Ubiquitin",
abstract = "Ubiquitin chains are formed through the action of a
set of enzymes that covalently link ubiquitin either
through peptide bonds or through isopeptide bonds
volume = "88",
number = "6",
pages = "4095--4106",
- keywords = "Animals",
- keywords = "Biophysics",
- keywords = "Elasticity",
- keywords = "Light",
- keywords = "Muscle Proteins",
- keywords = "Muscle, Skeletal",
- keywords = "Neutrons",
- keywords = "Protein Conformation",
- keywords = "Protein Kinases",
- keywords = "Rabbits",
- keywords = "Rheology",
- keywords = "Scattering, Radiation",
- keywords = "Temperature",
+ keywords = "Animals;Biophysics;Elasticity;Light;Muscle Proteins;Muscle, Skeletal;Neutrons;Protein Conformation;Protein Kinases;Rabbits;Rheology;Scattering, Radiation;Temperature",
abstract = "The persistence length of titin from rabbit skeletal
muscles was measured using a combination of static and
dynamic light scattering, and neutron small angle
volume = "94",
number = "7",
pages = "2621--2630",
- keywords = "Biotin",
- keywords = "Computer Simulation",
- keywords = "Elasticity",
- keywords = "Kinetics",
- keywords = "Mechanotransduction, Cellular",
- keywords = "Models, Chemical",
- keywords = "Models, Molecular",
- keywords = "Molecular Motor Proteins",
- keywords = "Motion",
- keywords = "Streptavidin",
- keywords = "Stress, Mechanical",
- keywords = "Transducers",
+ keywords = "Biotin;Computer Simulation;Elasticity;Kinetics;Mechanotransduction, Cellular;Models, Chemical;Models, Molecular;Molecular Motor Proteins;Motion;Streptavidin;Stress, Mechanical;Transducers",
abstract = "Forced unbinding of complementary macromolecules such
as ligand-receptor complexes can reveal energetic and
kinetic details governing physiological processes
year = "2001",
volume = "30",
pages = "105--128",
- keywords = "Biophysics",
- keywords = "Kinetics",
- keywords = "Microscopy, Atomic Force",
- keywords = "Models, Chemical",
- keywords = "Protein Binding",
- keywords = "Spectrum Analysis",
- keywords = "Time Factors",
+ keywords = "Biophysics;Kinetics;Microscopy, Atomic Force;Models, Chemical;Protein Binding;Spectrum Analysis;Time Factors",
abstract = "On laboratory time scales, the energy landscape of a
weak bond along a dissociation pathway is fully
explored through Brownian-thermal excitations, and
volume = "59",
number = "4",
pages = "861--872",
- keywords = "Cell Adhesion",
- keywords = "Erythrocyte Membrane",
- keywords = "Erythrocytes",
- keywords = "Hemagglutination",
- keywords = "Hemagglutinins",
- keywords = "Humans",
- keywords = "Kinetics",
- keywords = "Mathematics",
- keywords = "Models, Biological",
- keywords = "Pressure",
+ keywords = "Cell Adhesion;Erythrocyte Membrane;Erythrocytes;Hemagglutination;Hemagglutinins;Humans;Kinetics;Mathematics;Models, Biological;Pressure",
abstract = "An experimental method and analysis are introduced
which provide direct quantitation of the strength of
adhesive contact for large agglutinin-bonded regions
volume = "59",
number = "4",
pages = "849--860",
- keywords = "Animals",
- keywords = "Antibodies, Monoclonal",
- keywords = "Cell Adhesion",
- keywords = "Erythrocyte Membrane",
- keywords = "Erythrocytes",
- keywords = "Helix (Snails)",
- keywords = "Hemagglutination",
- keywords = "Hemagglutinins",
- keywords = "Humans",
- keywords = "Immune Sera",
- keywords = "Kinetics",
- keywords = "Lectins",
- keywords = "Mathematics",
+ keywords = "Animals;Antibodies, Monoclonal;Cell Adhesion;Erythrocyte Membrane;Erythrocytes;Helix (Snails);Hemagglutination;Hemagglutinins;Humans;Immune Sera;Kinetics;Lectins;Mathematics",
abstract = "As detailed in a companion paper (Berk, D., and E.
Evans. 1991. Biophys. J. 59:861-872), a method was
developed to quantitate the strength of adhesion
volume = "59",
number = "4",
pages = "838--848",
- keywords = "ABO Blood-Group System",
- keywords = "Animals",
- keywords = "Antibodies, Monoclonal",
- keywords = "Erythrocyte Deformability",
- keywords = "Erythrocyte Membrane",
- keywords = "Erythrocytes",
- keywords = "Glycophorin",
- keywords = "Helix (Snails)",
- keywords = "Hemagglutinins",
- keywords = "Humans",
- keywords = "Immune Sera",
- keywords = "Lectins",
- keywords = "Mathematics",
- keywords = "Models, Biological",
+ keywords = "ABO Blood-Group System;Animals;Antibodies, Monoclonal;Erythrocyte Deformability;Erythrocyte Membrane;Erythrocytes;Glycophorin;Helix (Snails);Hemagglutinins;Humans;Immune Sera;Lectins;Mathematics;Models, Biological",
abstract = "A simple micromechanical method has been developed to
measure the rupture strength of a molecular-point
attachment (focal bond) between two macroscopically
volume = 101,
number = 19,
pages = "7299--7304",
- keywords = "Kinetics",
- keywords = "Microscopy, Atomic Force",
- keywords = "Probability",
- keywords = "Ubiquitin",
+ keywords = "Kinetics;Microscopy, Atomic Force;Probability;Ubiquitin",
abstract = "We use single-molecule force spectroscopy to study the
kinetics of unfolding of the small protein ubiquitin.
Upon a step increase in the stretching force, a
volume = "334",
number = "1",
pages = "75--86",
- keywords = "Amino Acid Sequence",
- keywords = "Disulfides",
- keywords = "Humans",
- keywords = "Immunoglobulins",
- keywords = "Models, Molecular",
- keywords = "Molecular Sequence Data",
- keywords = "Muscle Proteins",
- keywords = "Myocardium",
- keywords = "Protein Denaturation",
- keywords = "Protein Engineering",
- keywords = "Protein Kinases",
- keywords = "Protein Structure, Tertiary",
- keywords = "Spectrum Analysis",
+ keywords = "Amino Acid Sequence;Disulfides;Humans;Immunoglobulins;Models, Molecular;Molecular Sequence Data;Muscle Proteins;Myocardium;Protein Denaturation;Protein Engineering;Protein Kinases;Protein Structure, Tertiary;Spectrum Analysis",
abstract = "The elastic I-band part of muscle protein titin
contains two tandem immunoglobulin (Ig) domain regions
of distinct mechanical properties. Until recently, the
volume = "345",
number = "4",
pages = "817--826",
- keywords = "Fibronectins",
- keywords = "Kinetics",
- keywords = "Microscopy, Atomic Force",
- keywords = "Models, Molecular",
- keywords = "Mutagenesis, Site-Directed",
- keywords = "Protein Denaturation",
- keywords = "Protein Folding",
- keywords = "Protein Structure, Tertiary",
- keywords = "Recombinant Fusion Proteins",
+ keywords = "Fibronectins;Kinetics;Microscopy, Atomic Force;Models, Molecular;Mutagenesis, Site-Directed;Protein Denaturation;Protein Folding;Protein Structure, Tertiary;Recombinant Fusion Proteins",
abstract = "Domain 10 of type III fibronectin (10FNIII) is known
to play a pivotal role in the mechanical interactions
between cell surface integrins and the extracellular
volume = "10",
number = "9",
pages = "731--737",
- keywords = "Anisotropy",
- keywords = "Escherichia coli",
- keywords = "Kinetics",
- keywords = "Models, Molecular",
- keywords = "Monte Carlo Method",
- keywords = "Protein Folding",
- keywords = "Protein Structure, Secondary",
- keywords = "Protein Structure, Tertiary",
- keywords = "Proteins",
- keywords = "Software",
- keywords = "Temperature",
- keywords = "Thermodynamics",
+ keywords = "Anisotropy;Escherichia coli;Kinetics;Models, Molecular;Monte Carlo Method;Protein Folding;Protein Structure, Secondary;Protein Structure, Tertiary;Proteins;Software;Temperature;Thermodynamics",
abstract = "Proteins show diverse responses when placed under
mechanical stress. The molecular origins of their
differing mechanical resistance are still unclear,
year = {1958},
month = {jun},
publisher = {American Statistical Association},
- copyright = {Copyright © 1958 American Statistical Association},
+ copyright = {Copyright \copy\ 1958 American Statistical Association},
}
@article{kellermayer03,
issn = "0005-2728",
doi = "10.1016/S0005-2728(03)00029-X",
url = "http://dx.doi.org/10.1016/S0005-2728(03)00029-X",
-author = "Miklós S. Z. Kellermayer and "# CBustamante #" and Henk L. Granzier",
-keywords = "Titin",
-keywords = "Wormlike chain",
-keywords = "Unfolding",
-keywords = "Elasticity",
-keywords = "AFM",
-keywords = "Molecular force spectroscopy",
+author = "Mikl\'os S. Z. Kellermayer and "# CBustamante #" and Henk L. Granzier",
+ keywords = "Titin;Wormlike chain;Unfolding;Elasticity;AFM;Molecular force spectroscopy",
abstract = "
Titin is a giant polypeptide that spans half of the striated muscle sarcomere and generates passive force upon stretch. To explore the elastic response and structure of single molecules and oligomers of titin, we carried out molecular force spectroscopy and atomic force microscopy (AFM) on purified full-length skeletal-muscle titin. From the force data, apparent persistence lengths as long as ~1.5 nm were obtained for the single, unfolded titin molecule. Furthermore, data suggest that titin molecules may globally associate into oligomers which mechanically behave as independent wormlike chains (WLCs). Consistent with this, AFM of surface-adsorbed titin molecules revealed the presence of oligomers. Although oligomers may form globally via head-to-head association of titin, the constituent molecules otherwise appear independent from each other along their contour. Based on the global association but local independence of titin molecules, we discuss a mechanical model of the sarcomere in which titin molecules with different contour lengths, corresponding to different isoforms, are held in a lattice. The net force response of aligned titin molecules is determined by the persistence length of the tandemly arranged, different WLC components of the individual molecules, the ratio of their overall contour lengths, and by domain unfolding events. Biased domain unfolding in mechanically selected constituent molecules may serve as a compensatory mechanism for contour- and persistence-length differences. Variation in the ratio and contour length of the component chains may provide mechanisms for the fine-tuning of the sarcomeric passive force response."
}
volume = 99,
number = 18,
pages = "11682--11687",
- keywords = "DNA-Directed RNA Polymerases",
- keywords = "Escherichia coli",
- keywords = "Kinetics",
- keywords = "Transcription, Genetic",
+ keywords = "DNA-Directed RNA Polymerases;Escherichia coli;Kinetics;Transcription, Genetic",
abstract = "Escherichia coli RNA polymerase translocates along the
DNA discontinuously during the elongation phase of
transcription, spending proportionally more time at
volume = 397,
number = 6714,
pages = "50--53",
- keywords = "Biotin",
- keywords = "Microscopy, Atomic Force",
- keywords = "Protein Binding",
- keywords = "Streptavidin",
+ keywords = "Biotin;Microscopy, Atomic Force;Protein Binding;Streptavidin",
abstract = "Atomic force microscopy (AFM) has been used to measure
the strength of bonds between biological receptor
molecules and their ligands. But for weak noncovalent
volume = 303,
number = 5664,
pages = "1674--1678",
- keywords = "Chemistry, Physical",
- keywords = "Microscopy, Atomic Force",
- keywords = "Physicochemical Phenomena",
- keywords = "Polyubiquitin",
- keywords = "Protein Conformation",
- keywords = "Protein Denaturation",
- keywords = "Protein Folding",
- keywords = "Protein Structure, Secondary",
- keywords = "Time Factors",
- keywords = "Ubiquitin",
+ keywords = "Chemistry, Physical;Microscopy, Atomic Force;Physicochemical Phenomena;Polyubiquitin;Protein Conformation;Protein Denaturation;Protein Folding;Protein Structure, Secondary;Time Factors;Ubiquitin",
abstract = "We used force-clamp atomic force microscopy to measure
the end-to-end length of the small protein ubiquitin
during its folding reaction at the single-molecule
volume = 385,
number = 4,
pages = "1277--1286",
- keywords = "Animals",
- keywords = "Biomechanics",
- keywords = "Cattle",
- keywords = "Fibronectins",
- keywords = "Kinetics",
- keywords = "Microscopy, Atomic Force",
- keywords = "Protein Folding",
- keywords = "Protein Structure, Tertiary",
- keywords = "Spectrum Analysis",
- keywords = "Tenascin",
+ keywords = "Animals;Biomechanics;Cattle;Fibronectins;Kinetics;Microscopy, Atomic Force;Protein Folding;Protein Structure, Tertiary;Spectrum Analysis;Tenascin",
abstract = "Tenascin-X is an extracellular matrix protein and
binds a variety of molecules in extracellular matrix
and on cell membrane. Tenascin-X plays important roles
volume = 74,
number = "1-2",
pages = "63--91",
- keywords = "Elasticity",
- keywords = "Hydrogen Bonding",
- keywords = "Microscopy, Atomic Force",
- keywords = "Protein Denaturation",
- keywords = "Protein Engineering",
- keywords = "Protein Folding",
- keywords = "Recombinant Proteins",
- keywords = "Signal Processing, Computer-Assisted",
+ keywords = "Elasticity;Hydrogen Bonding;Microscopy, Atomic Force;Protein Denaturation;Protein Engineering;Protein Folding;Recombinant Proteins;Signal Processing, Computer-Assisted",
abstract = "Mechanical unfolding and refolding may regulate the
molecular elasticity of modular proteins with
mechanical functions. The development of the atomic
volume = 106,
number = 8,
pages = "2677--2682",
- keywords = "Genome",
- keywords = "Introns",
- keywords = "Phylogeny",
+ keywords = "Genome;Introns;Phylogeny",
abstract = "For comparison of whole-genome (genic + nongenic)
sequences, multiple sequence alignment of a few
selected genes is not appropriate. One approach is to
volume = "37",
number = "1",
pages = "145--151",
- keywords = "divergence",
- keywords = "dissimilarity measure",
- keywords = "discrimintation information",
- keywords = "entropy",
- keywords = "probability of error bounds",
+ keywords = "divergence;dissimilarity measure;discrimintation information;entropy;probability of error bounds",
abstract = "A novel class of information-theoretic divergence
measures based on the Shannon entropy is
introduced. Unlike the well-known Kullback
volume = 73,
number = 4,
pages = "2043--2053",
- keywords = "Amino Acid Sequence",
- keywords = "Animals",
- keywords = "Biomechanics",
- keywords = "Biophysical Phenomena",
- keywords = "Biophysics",
- keywords = "Cell Fractionation",
- keywords = "Elasticity",
- keywords = "Gelsolin",
- keywords = "Microscopy, Immunoelectron",
- keywords = "Models, Cardiovascular",
- keywords = "Molecular Structure",
- keywords = "Muscle Proteins",
- keywords = "Myocardial Contraction",
- keywords = "Myocardium",
- keywords = "Protein Kinases",
- keywords = "Rats",
- keywords = "Sarcomeres",
+ keywords = "Amino Acid Sequence;Animals;Biomechanics;Biophysical Phenomena;Biophysics;Cell Fractionation;Elasticity;Gelsolin;Microscopy, Immunoelectron;Models, Cardiovascular;Molecular Structure;Muscle Proteins;Myocardial Contraction;Myocardium;Protein Kinases;Rats;Sarcomeres",
abstract = "Titin (also known as connectin) is a giant filamentous
protein whose elastic properties greatly contribute to
the passive force in muscle. In the sarcomere, the
number = 24,
pages = 248301,
keywords = "Kinetics",
- keywords = "Microscopy, Atomic Force",
- keywords = "Models, Chemical",
- keywords = "Muscle Proteins",
- keywords = "Protein Conformation",
- keywords = "Protein Folding",
- keywords = "Protein Kinases",
- keywords = "Protein Structure, Tertiary",
- keywords = "Thermodynamics",
+ keywords = "Microscopy, Atomic Force;Models, Chemical;Muscle Proteins;Protein Conformation;Protein Folding;Protein Kinases;Protein Structure, Tertiary;Thermodynamics",
abstract = "Single-molecule manipulation has allowed the forced
unfolding of multidomain proteins. Here we outline a
theory that not only explains these experiments but
volume = "130",
number = "12",
pages = "3706--3707",
- keywords = "Computer Simulation",
- keywords = "Kinetics",
- keywords = "Models, Chemical",
- keywords = "Protein Folding",
- keywords = "Stress, Mechanical",
- keywords = "Ubiquitin",
+ keywords = "Computer Simulation;Kinetics;Models, Chemical;Protein Folding;Stress, Mechanical;Ubiquitin",
abstract = "Despite a large number of studies on the mechanical
unfolding of proteins, there are still relatively few
successful attempts to refold proteins in the presence
volume = "112",
number = "19",
pages = "5968--5976",
- keywords = "Computer Simulation",
- keywords = "Kinetics",
- keywords = "Models, Molecular",
- keywords = "Protein Folding",
- keywords = "Protein Structure, Tertiary",
- keywords = "Time Factors",
- keywords = "Ubiquitin",
+ keywords = "Computer Simulation;Kinetics;Models, Molecular;Protein Folding;Protein Structure, Tertiary;Time Factors;Ubiquitin",
abstract = "The folding and unfolding kinetics of single
molecules, such as proteins or nucleic acids, can be
explored by mechanical pulling experiments. Determining
eid = 063701,
numpages = 5,
pages = 063701,
-keywords = {calibration; vibration measurement; measurement by laser beam; Doppler measurement; measurement uncertainty; atomic force microscopy},
+ keywords = {calibration; vibration measurement; measurement by laser beam; Doppler measurement; measurement uncertainty; atomic force microscopy},
url = {http://link.aip.org/link/?RSI/78/063701/1},
doi = {10.1063/1.2743272},
project = "Cantilever Calibration",
pages = "355--361",
year = 2005,
issn = "0301-679X",
-keywords = "AFM",
-keywords = "Liquid",
-keywords = "Hydrodynamic",
-keywords = "Lubrication",
+keywords = "AFM;Liquid;Hydrodynamic;Lubrication",
abstract = "With the availability of equipment used in Scanning Probe
Microscopy (SPM), researchers have been able to probe the local
fluid-substrate force interactions with resolutions of pN using a
volume = 409,
number = 6822,
pages = "824--826",
- keywords = "Amino Acid Sequence",
- keywords = "Chromosome Mapping",
- keywords = "Computational Biology",
- keywords = "Genes",
- keywords = "Genetic Variation",
- keywords = "Genome, Human",
- keywords = "Human Genome Project",
- keywords = "Humans",
- keywords = "Internet",
- keywords = "Molecular Sequence Data",
- keywords = "Sequence Analysis, DNA",
+ keywords = "Amino Acid Sequence;Chromosome Mapping;Computational Biology;Genes;Genetic Variation;Genome, Human;Human Genome Project;Humans;Internet;Molecular Sequence Data;Sequence Analysis, DNA",
abstract = "There are a number of ways to investigate the
structure, function and evolution of the human genome.
These include examining the morphology of normal and
volume = 409,
number = 6822,
pages = "934--941",
- keywords = "Chromosomes, Artificial, Bacterial",
- keywords = "Cloning, Molecular",
- keywords = "Contig Mapping",
- keywords = "DNA Fingerprinting",
- keywords = "Gene Duplication",
- keywords = "Genome, Human",
- keywords = "Humans",
- keywords = "In Situ Hybridization, Fluorescence",
- keywords = "Repetitive Sequences, Nucleic Acid",
+ keywords = "Chromosomes, Artificial, Bacterial;Cloning, Molecular;Contig Mapping;DNA Fingerprinting;Gene Duplication;Genome, Human;Humans;In Situ Hybridization, Fluorescence;Repetitive Sequences, Nucleic Acid",
abstract = "The human genome is by far the largest genome to be
sequenced, and its size and complexity present many
challenges for sequence assembly. The International
volume=291,
number=5507,
pages="1304--1351",
-keywords="Algorithms",
-keywords="Animals",
-keywords="Chromosome Banding",
-keywords="Chromosome Mapping",
-keywords="Chromosomes, Artificial, Bacterial",
-keywords="Computational Biology",
-keywords="Consensus Sequence",
-keywords="CpG Islands",
-keywords="DNA, Intergenic",
-keywords="Databases, Factual",
-keywords="Evolution, Molecular",
-keywords="Exons",
-keywords="Female",
-keywords="Gene Duplication",
-keywords="Genes",
-keywords="Genetic Variation",
-keywords="Genome, Human",
-keywords="Human Genome Project",
-keywords="Humans",
-keywords="Introns",
-keywords="Male",
-keywords="Phenotype",
-keywords="Physical Chromosome Mapping",
-keywords="Polymorphism, Single Nucleotide",
-keywords="Proteins",
-keywords="Pseudogenes",
-keywords="Repetitive Sequences, Nucleic Acid",
-keywords="Retroelements",
-keywords="Sequence Analysis, DNA",
-keywords="Species Specificity",
+ keywords = "Algorithms;Animals;Chromosome Banding;Chromosome Mapping;Chromosomes, Artificial, Bacterial;Computational Biology;Consensus Sequence;CpG Islands;DNA, Intergenic;Databases, Factual;Evolution, Molecular;Exons;Female;Gene Duplication;Genes;Genetic Variation;Genome, Human;Human Genome Project;Humans;Introns;Male;Phenotype;Physical Chromosome Mapping;Polymorphism, Single Nucleotide;Proteins;Pseudogenes;Repetitive Sequences, Nucleic Acid;Retroelements;Sequence Analysis, DNA;Species Specificity",
abstract="A 2.91-billion base pair (bp) consensus sequence of the
euchromatic portion of the human genome was generated by the
whole-genome shotgun sequencing method. The 14.8-billion bp DNA
volume = 291,
number = 5507,
pages = "1255--1257",
- keywords = "Animals",
- keywords = "Computational Biology",
- keywords = "Drug Industry",
- keywords = "Expressed Sequence Tags",
- keywords = "Gene Expression",
- keywords = "Gene Expression Regulation",
- keywords = "Genes",
- keywords = "Genetic Techniques",
- keywords = "Genome, Human",
- keywords = "Genomics",
- keywords = "Human Genome Project",
- keywords = "Humans",
- keywords = "Models, Genetic",
- keywords = "Polymorphism, Single Nucleotide",
- keywords = "Proteins",
- keywords = "RNA, Messenger",
+ keywords = "Animals;Computational Biology;Drug Industry;Expressed Sequence Tags;Gene Expression;Gene Expression Regulation;Genes;Genetic Techniques;Genome, Human;Genomics;Human Genome Project;Humans;Models, Genetic;Polymorphism, Single Nucleotide;Proteins;RNA, Messenger",
ISSN = "0036-8075",
url = "http://www.sciencemag.org/cgi/content/full/291/5507/1255",
}
volume = 300,
number = 5617,
pages = "286--290",
- keywords = "Access to Information",
- keywords = "Computational Biology",
- keywords = "Databases, Nucleic Acid",
- keywords = "Genome, Human",
- keywords = "Genomics",
- keywords = "Government Agencies",
- keywords = "History, 20th Century",
- keywords = "Human Genome Project",
- keywords = "Humans",
- keywords = "International Cooperation",
- keywords = "National Institutes of Health (U.S.)",
- keywords = "Private Sector",
- keywords = "Public Policy",
- keywords = "Public Sector",
- keywords = "Publishing",
- keywords = "Quality Control",
- keywords = "Sequence Analysis, DNA",
- keywords = "United States",
+ keywords = "Access to Information;Computational Biology;Databases, Nucleic Acid;Genome, Human;Genomics;Government Agencies;History, 20th Century;Human Genome Project;Humans;International Cooperation;National Institutes of Health (U.S.);Private Sector;Public Policy;Public Sector;Publishing;Quality Control;Sequence Analysis, DNA;United States",
ISSN = "1095-9203",
doi = "10.1126/science.1084564",
url = "http://www.sciencemag.org/cgi/content/summary/300/5617/277",
volume = 89,
number = 1,
pages = "20--22",
- keywords = "Mathematics",
- keywords = "Models, Theoretical",
- keywords = "Protein Conformation",
- keywords = "Proteins",
+ keywords = "Mathematics;Models, Theoretical;Protein Conformation;Proteins",
abstract = "Levinthal's paradox is that finding the native folded
state of a protein by a random search among all
possible configurations can take an enormously long
volume = 6,
number = 6,
pages = "1157--1166",
- keywords = "Allosteric Regulation",
- keywords = "Bacterial Proteins",
- keywords = "Binding Sites",
- keywords = "Biotin",
- keywords = "Crystallography, X-Ray",
- keywords = "Hydrogen Bonding",
- keywords = "Ligands",
- keywords = "Models, Molecular",
- keywords = "Molecular Conformation",
- keywords = "Streptavidin",
- keywords = "Tryptophan",
+ keywords = "Allosteric Regulation;Bacterial Proteins;Binding Sites;Biotin;Crystallography, X-Ray;Hydrogen Bonding;Ligands;Models, Molecular;Molecular Conformation;Streptavidin;Tryptophan",
abstract = "The streptavidin-biotin complex provides the basis for
many important biotechnological applications and is an
interesting model system for studying high-affinity
volume = 4,
number = 3,
pages = "323--337",
- keywords = "Amino Acid Sequence",
- keywords = "Immunoglobulins",
- keywords = "Magnetic Resonance Spectroscopy",
- keywords = "Models, Molecular",
- keywords = "Molecular Sequence Data",
- keywords = "Molecular Structure",
- keywords = "Muscle Proteins",
- keywords = "Protein Kinases",
- keywords = "Protein Structure, Secondary",
- keywords = "Protein Structure, Tertiary",
- keywords = "Sequence Alignment",
+ keywords = "Amino Acid Sequence;Immunoglobulins;Magnetic Resonance Spectroscopy;Models, Molecular;Molecular Sequence Data;Molecular Structure;Muscle Proteins;Protein Kinases;Protein Structure, Secondary;Protein Structure, Tertiary;Sequence Alignment",
abstract = "BACKGROUND. The giant muscle protein titin forms a
filament which spans half of the sarcomere and
performs, along its length, quite diverse functions.
volume = 38,
number = "Database issue",
pages = "D142--D148",
- keywords = "Algorithms",
- keywords = "Animals",
- keywords = "Computational Biology",
- keywords = "Databases, Nucleic Acid",
- keywords = "Databases, Protein",
- keywords = "Europe",
- keywords = "Genome, Fungal",
- keywords = "Genome, Viral",
- keywords = "Humans",
- keywords = "Information Storage and Retrieval",
- keywords = "Internet",
- keywords = "Protein Isoforms",
- keywords = "Proteome",
- keywords = "Proteomics",
- keywords = "Software",
+ keywords = "Algorithms;Animals;Computational Biology;Databases, Nucleic Acid;Databases, Protein;Europe;Genome, Fungal;Genome, Viral;Humans;Information Storage and Retrieval;Internet;Protein Isoforms;Proteome;Proteomics;Software",
abstract = "The primary mission of UniProt is to support
biological research by maintaining a stable,
comprehensive, fully classified, richly and accurately
volume = 170,
number = 3,
pages = "1236--1241",
- keywords = "Amino Acid Sequence",
- keywords = "Animals",
- keywords = "Bacterial Proteins",
- keywords = "Binding Sites",
- keywords = "Cell Line",
- keywords = "Cell Membrane",
- keywords = "Cricetinae",
- keywords = "Fibronectins",
- keywords = "Molecular Sequence Data",
- keywords = "Streptavidin",
+ keywords = "Amino Acid Sequence;Animals;Bacterial Proteins;Binding Sites;Cell Line;Cell Membrane;Cricetinae;Fibronectins;Molecular Sequence Data;Streptavidin",
abstract = "Streptavidin binds at low levels and high affinity to
cell surfaces, the cause of which can be traced to the
occurrence of a sequence containing RYD (Arg-Tyr-Asp)
volume = 4,
number = 1,
pages = "10--19",
- keywords = "Kinetics",
- keywords = "Models, Chemical",
- keywords = "Protein Folding",
+ keywords = "Kinetics;Models, Chemical;Protein Folding",
abstract = "While the classical view of protein folding kinetics
relies on phenomenological models, and regards folding
intermediates in a structural way, the new view
volume = 105,
number = 20,
pages = "7182--7187",
- keywords = "Biochemistry",
- keywords = "Guanidine",
- keywords = "Kinetics",
- keywords = "Micrococcal Nuclease",
- keywords = "Models, Biological",
- keywords = "Models, Chemical",
- keywords = "Models, Theoretical",
- keywords = "Protein Conformation",
- keywords = "Protein Denaturation",
- keywords = "Protein Folding",
- keywords = "Protein Structure, Secondary",
- keywords = "Proteins",
- keywords = "Proteomics",
- keywords = "Reproducibility of Results",
- keywords = "Thermodynamics",
+ keywords = "Biochemistry;Guanidine;Kinetics;Micrococcal Nuclease;Models, Biological;Models, Chemical;Models, Theoretical;Protein Conformation;Protein Denaturation;Protein Folding;Protein Structure, Secondary;Proteins;Proteomics;Reproducibility of Results;Thermodynamics",
abstract = "The observation of heterogeneous protein folding
kinetics has been widely interpreted in terms of
multiple independent unrelated pathways (IUP model),
volume = 95,
number = 1,
pages = "426--434",
- keywords = "Algorithms",
- keywords = "Computer Simulation",
- keywords = "Microscopy, Atomic Force",
- keywords = "Models, Chemical",
- keywords = "Models, Molecular",
- keywords = "Protein Denaturation",
- keywords = "Protein Folding",
- keywords = "Proteins",
+ keywords = "Algorithms;Computer Simulation;Microscopy, Atomic Force;Models, Chemical;Models, Molecular;Protein Denaturation;Protein Folding;Proteins",
abstract = "Single molecule force spectroscopy has evolved into an
important and extremely powerful technique for
investigating the folding potentials of biomolecules.
pages = "159--166",
year = 2010,
issn = "0141-8130",
-keywords = "Atomic force microscopy",
-keywords = "Mechanical unfolding",
-keywords = "Monte Carlo simulation",
-keywords = "Worm-like chain",
-keywords = "Single molecule methods",
+keywords = "Atomic force microscopy;Mechanical unfolding;Monte Carlo simulation;Worm-like chain;Single molecule methods",
abstract = "Single molecule methods are becoming routine biophysical
techniques for studying biological macromolecules. In mechanical
unfolding of proteins, an externally applied force is used to induce
projects / thesis.git / commitdiff