pages = "1236--1241",
issn = "0006-291X",
doi = "DOI: 10.1016/0006-291X(90)90526-S",
- url = "http://www.sciencedirect.com/science/article/B6WBK-
- 4F5M7K3-3C/2/c94b612e06efc8534ee24bb1da889811",
+ url = "http://www.sciencedirect.com/science/article/B6WBK-4F5M7K3-3C/2/c94b612e06efc8534ee24bb1da889811",
keywords = "Amino Acid Sequence;Animals;Bacterial Proteins;Binding
Sites;Cell Line;Cell Membrane;Cricetinae;Fibronectins;Molecular
Sequence Data;Streptavidin",
pages = "101--125",
issn = "0066-4154",
doi = "10.1146/annurev.biochem.77.060706.093102",
- eprint = "http://arjournals.annualreviews.org/doi/pdf/10.1146/annurev.bioch
- em.77.060706.093102",
- url = "http://arjournals.annualreviews.org/doi/abs/10.1146/annurev.biochem.
- 77.060706.093102",
+ eprint = "http://arjournals.annualreviews.org/doi/pdf/10.1146/annurev.biochem.77.060706.093102",
+ url = "http://arjournals.annualreviews.org/doi/abs/10.1146/annurev.biochem.77.060706.093102",
abstract = "Although protein-folding studies began several decades ago, it
is only recently that the tools to analyze protein folding at the
single-molecule level have been developed. Advances in single-molecule
pages = "45--50",
issn = "0066-4154",
doi = "10.1146/annurev.biochem.012108.120952",
- eprint = "http://arjournals.annualreviews.org/doi/pdf/10.1146/annurev.bioch
- em.012108.120952",
- url = "http://arjournals.annualreviews.org/doi/abs/10.1146/annurev.biochem.
- 012108.120952",
+ eprint = "http://arjournals.annualreviews.org/doi/pdf/10.1146/annurev.biochem.012108.120952",
+ url = "http://arjournals.annualreviews.org/doi/abs/10.1146/annurev.biochem.012108.120952",
abstract = "It has been over one-and-a-half decades since methods of
single-molecule detection and manipulation were first introduced in
biochemical research. Since then, the application of these methods to
number = "1-2",
pages = "63--91",
issn = "0079-6107",
- eprint = "http://www.pubmedcentral.nih.gov/picrender.fcgi?artid=1302160&blo
- btype=pdf",
+ eprint = "http://www.pubmedcentral.nih.gov/picrender.fcgi?artid=1302160&blobtype=pdf",
url = "http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=1302160",
keywords = "Elasticity;Hydrogen Bonding;Microscopy, Atomic Force;Protein
Denaturation;Protein Engineering;Protein Folding;Recombinant
pages = "105--128",
issn = "1056-8700",
doi = "10.1146/annurev.biophys.30.1.105",
- url = "http://arjournals.annualreviews.org/doi/abs/10.1146%2Fannurev.biophy
- s.30.1.105",
+ url = "http://arjournals.annualreviews.org/doi/abs/10.1146%2Fannurev.biophys.30.1.105",
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
pages = "895--901",
issn = "0956-5663",
doi = "10.1016/0956-5663(95)99227-C",
- url = "http://www.sciencedirect.com/science/article/B6TFC-
- 3XY2HK9-G/2/6f4e9f67e9a1e14c8bbcc478e5360682",
+ url = "http://www.sciencedirect.com/science/article/B6TFC-3XY2HK9-G/2/6f4e9f67e9a1e14c8bbcc478e5360682",
abstract = "One of the unique features of the atomic force microscope (AFM)
is its capacity to measure interactions between tip and sample with
high sensitivity and unparal leled spatial resolution. Since the
pages = "3212--3237",
issn = "1521-3773",
doi = "10.1002/1521-3773(20000915)39:18<3212::AID-ANIE3212>3.0.CO;2-X",
- eprint = "",
- url = "http://dx.doi.org/10.1002/1521-3773(20000915)39:18<3212::AID-
- ANIE3212>3.0.CO;2-X",
+ url = "http://dx.doi.org/10.1002/1521-3773(20000915)39:18<3212::AID-ANIE3212>3.0.CO;2-X",
abstract = "How do molecules interact with each other? What happens if a
neurotransmitter binds to a ligand-operated ion channel? How do
antibodies recognize their antigens? Molecular recognition events play
pages = "355--361",
issn = "0301-679X",
doi = "DOI: 10.1016/j.triboint.2004.08.016",
- url = "http://www.sciencedirect.com/science/article/B6V57-4DN9K7J-1/2/fef91
- ac022594c2c6a701376d83ecd31",
+ url = "http://www.sciencedirect.com/science/article/B6V57-4DN9K7J-1/2/fef91ac022594c2c6a701376d83ecd31",
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-
pages = "159--166",
issn = "0141-8130",
doi = "10.1016/j.ijbiomac.2009.12.001",
- url = "http://www.sciencedirect.com/science/article/B6T7J-
- 4XWMND2-1/2/7ef768562b4157fc201d450553e5de5e",
+ url = "http://www.sciencedirect.com/science/article/B6T7J-4XWMND2-1/2/7ef768562b4157fc201d450553e5de5e",
keywords = "Atomic force microscopy;Mechanical unfolding;Monte Carlo
simulation;Worm-like chain;Single molecule methods",
abstract = "Single molecule methods are becoming routine biophysical
pages = "145--151",
issn = "0018-9448",
doi = "10.1109/18.61115",
- url = "http://ieeexplore.ieee.org/xpl/freeabs_all.jsp?isnumber=2227&arnumbe
- r=61115&count=35&index=9",
+ url = "http://ieeexplore.ieee.org/xpl/freeabs_all.jsp?isnumber=2227&arnumber=61115&count=35&index=9",
keywords = "divergence;dissimilarity measure;discrimintation
information;entropy;probability of error bounds",
abstract = "A novel class of information-theoretic divergence measures
pages = "453--463",
issn = "0887-3585",
doi = "10.1002/(SICI)1097-0134(19990601)35:4<453::AID-PROT9>3.0.CO;2-M",
- eprint = "http://www3.interscience.wiley.com/cgi-
- bin/fulltext/65000328/PDFSTART",
+ eprint = "http://www3.interscience.wiley.com/cgi-bin/fulltext/65000328/PDFSTART",
url = "http://www3.interscience.wiley.com/journal/65000328/abstract",
keywords = "Computer Simulation;Fibronectins;Hydrogen Bonding;Microscopy,
Atomic Force;Models, Molecular;Protein Denaturation",
pages = "9663--9673",
publisher = AIP,
doi = "10.1063/1.1369622",
- eprint = "http://hansmalab.physics.ucsb.edu/pdf/297%20-%20Makarov,%20D.E._J
- .Chem.Phys._2001.pdf",
+ eprint = "http://hansmalab.physics.ucsb.edu/pdf/297%20-%20Makarov,%20D.E._J.Chem.Phys._2001.pdf",
url = "http://link.aip.org/link/?JCP/114/9663/1",
keywords = "proteins; hydrogen bonds; digital simulation; Monte Carlo
methods; molecular biophysics; intramolecular mechanics;
number = 26,
pages = "8759--8770",
issn = "0024-9297",
- eprint = "http://pubs.acs.org/cgi-
- bin/archive.cgi/mamobx/1995/28/i26/pdf/ma00130a008.pdf",
+ eprint = "http://pubs.acs.org/cgi-bin/archive.cgi/mamobx/1995/28/i26/pdf/ma00130a008.pdf",
url =
- "http://pubs3.acs.org/acs/journals/doilookup?in_doi=10.1021/ma00130a008
- ",
- abstract = "",
+ "http://pubs3.acs.org/acs/journals/doilookup?in_doi=10.1021/ma00130a008",
note = "Derivation of the Worm-like Chain interpolation function."
}
pages = "20--22",
issn = "0027-8424",
eprint =
- "http://www.ncbi.nlm.nih.gov/pmc/articles/PMC48166/pdf/pnas01075-0036.p
- df",
+ "http://www.ncbi.nlm.nih.gov/pmc/articles/PMC48166/pdf/pnas01075-0036.pdf",
url = "http://www.ncbi.nlm.nih.gov/pmc/articles/PMC48166/",
keywords = "Mathematics;Models, Theoretical;Protein Conformation;Proteins",
abstract = "Levinthal's paradox is that finding the native folded state of
projects / thesis.git / commitdiff