@string{DAbramavicius = "Abramavicius, Darius"}
@string{JFAbril = "Abril, J. F."}
@string{JAbu-Threideh = "Abu-Threideh, J."}
+@string{KAdachi = "Adachi, Kengo"}
@string{MDAdams = "Adams, M. D."}
@string{AdvExpMedBiol = "Adv Exp Med Biol"}
@string{SAinavarapu = "Ainavarapu, Sri Rama Koti"}
@string{ASA = "American Statistical Association"}
@string{HAn = "An, H."}
@string{KNAn = "An, Kai-Nan"}
+@string{ABioChem = "Analytical biochemistry"}
@string{IAndricioaei = "Andricioaei, Ioan"}
@string{ACIEE = "Angew. Chem. Int. Ed. Engl."}
@string{ARBBS = "Annu Rev Biophys Biomol Struct"}
@string{ARBC = "Annual Review of Biochemistry"}
-@string{DAnselmetti = "Anselmetti, D."}
+@string{DAnselmetti = "Anselmetti, Dario"}
@string{AMC = "Applied Mathematics and Computation"}
@string{SArcidiacono = "Arcidiacono, S"}
@string{CArciola = "Arciola, Carla Renata"}
@string{AAwe = "Awe, A."}
@string{SBedard = "B\'edard, Sabrina"}
@string{WBaase = "Baase, Walter A."}
+@string{YBaba = "Baba, Y."}
@string{HBaden = "Baden, H."}
@string{CBadilla = "Badilla, Carmen L."}
@string{VBafna = "Bafna, V."}
@string{MBarnstead = "Barnstead, M."}
@string{DBarrick = "Barrick, Doug"}
@string{IBarrow = "Barrow, I."}
-@string{FWBartels = "Bartels, F. W."}
+@string{FWBartels = "Bartels, Frank Wilco"}
@string{BBarz = "Barz, Bogdan"}
@string{TBasche = "Basche, Th."}
@string{ABasu = "Basu, A."}
@string{LBaugh = "Baugh, Loren"}
+@string{BBaumgarth = "Baumgarth, Birgit"}
@string{SBaumhueter = "Baumhueter, S."}
@string{JBaxendale = "Baxendale, J."}
@string{EABayer = "Bayer, Edward A."}
@string{EBeasley = "Beasley, E."}
@string{JBechhoefer = "Bechhoefer, John"}
+@string{ABecker = "Becker, Anke"}
@string{GSBeddard = "Beddard, Godfrey S."}
+@string{TBeebe = "Beebe, Thomas P."}
@string{KBeeson = "Beeson, K."}
@string{GIBell = "Bell, G. I."}
@string{FBenedetti = "Benedetti, Fabrizio"}
@string{Biochem = "Biochemistry"}
@string{BBABE = "Biochimica et Biophysica Acta (BBA) - Bioenergetics"}
@string{BIOINFO = "Bioinformatics (Oxford, England)",}
-@string{BPJ = "Biophys. J."}
+@string{BPJ = "Biophysical Journal"}
+%@string{BPJ = "Biophys. J."}
@string{BIOSENSE = "Biosensors and Bioelectronics"}
@string{BIOTECH = "Biotechnology and Bioengineering"}
@string{JBirchler = "Birchler, James A."}
@string{DJBrockwell = "Brockwell, David J."}
@string{SBroder = "Broder, S."}
@string{SBroedel = "Broedel, Sheldon E."}
+@string{ABrolo = "Brolo, Alexandre G."}
@string{BrooksCole = "Brooks/Cole"}
@string{BDBrowerToland = "Brower-Toland, Brent D."}
@string{MBrucale = "Brucale, Marco"}
@string{ABuguin = "Buguin, A."}
@string{ABulhassan = "Bulhassan, Ahmed"}
@string{BBullard = "Bullard, Belinda"}
+@string{RBunk = "Bunk, Richard"}
@string{DBusam = "Busam, D."}
@string{CBustamante = "Bustamante, Carlos"}
@string{YBustanji = "Bustanji, Yasser"}
@string{KChaturvedi = "Chaturvedi, K."}
@string{CChauzy = "Chauzy, C."}
@string{SChe = "Che, Shunai"}
+@string{CHEMREV = "Chemical reviews"}
@string{CHEM = "Chemistry (Weinheim an der Bergstrasse, Germany)"}
@string{CPC = "Chemphyschem"}
@string{HCChen = "Chen, H. C."}
@string{VGCheung = "Cheung, V. G."}
@string{YHChiang = "Chiang, Y. H."}
@string{AChinwalla = "Chinwalla, A."}
+@string{FChow = "Chow, Flora"}
@string{JChoy = "Choy, Jason"}
@string{BChu = "Chu, Benjamin"}
@string{XChu = "Chu, Xueying"}
@string{WDeGrado = "DeGrado, William F."}
@string{PDebrunner = "Debrunner, P."}
@string{ADelcher = "Delcher, A."}
+@string{WDeLorbe = "DeLorbe, William J."}
@string{BDelpech = "Delpech, B."}
@string{Demography = "Demography"}
@string{ZDeng = "Deng, Z."}
@string{RFulton = "Fulton, R."}
@string{TFunck = "Funck, Theodor"}
@string{TFurey = "Furey, T."}
+@string{SFuruike = "Furuike, Shou"}
@string{GLGaborMiklos = "Gabor Miklos, G. L."}
@string{AEGabrielian = "Gabrielian, A. E."}
@string{WGan = "Gan, W."}
@string{LAGavrilov = "Gavrilov, L. A."}
@string{NSGavrilova = "Gavrilova, N. S."}
@string{WGe = "Ge, W."}
+@string{GENE = "Gene"}
@string{CGergely = "Gergely, C."}
@string{RGibbs = "Gibbs, R."}
@string{DGilbert = "Gilbert, D."}
@string{FGong = "Gong, F."}
@string{MGorokhov = "Gorokhov, M."}
@string{JHGorrell = "Gorrell, J. H."}
-@string{AGrutzner = {Gr\"utzner, Anika}}
@string{KGraham = "Graham, K."}
@string{HLGranzier = "Granzier, Henk L."}
-@string{FGrater = "Grater, Frauke"}
+@string{FGrater = "Gr{\"a}ter, Frauke"}
@string{EDGreen = "Green, E. D."}
@string{SGGregory = "Gregory, S. G."}
@string{BGropman = "Gropman, B."}
@string{CGrossman = "Grossman, C."}
@string{HGrubmuller = {Grubm\"uller, Helmut}}
+@string{AGrutzner = {Gr\"utzner, Anika}}
@string{ZGu = "Gu, Z."}
@string{PGuan = "Guan, P."}
@string{RGuigo = "Guig\'o, R."}
@string{PHanggi = {H\"anggi, Peter}}
@string{THa = "Ha, Taekjip"}
@string{JHaack = "Haack, Julie A."}
+@string{GHager = "Hager, Gabriele"}
@string{RHajjar = "Hajjar, Roger J."}
@string{AHalpern = "Halpern, A."}
@string{KHalvorsen = "Halvorsen, Ken"}
@string{SHannenhalli = "Hannenhalli, S."}
@string{HHansma = "Hansma, H. G."}
@string{PHansma = "Hansma, Paul K."}
+@string{DHarbrecht = "Harbrecht, Douglas"}
@string{SHarper = "Harper, Sandy"}
@string{MHarris = "Harris, M."}
@string{BHart = "Hart, B."}
@string{JHemmerle = "Hemmerle, J."}
@string{SHenderson = "Henderson, S."}
@string{BHeymann = "Heymann, Berthold"}
+@string{NHiaro = "Hiaro, N."
@string{MEHiggins = "Higgins, M. E."}
@string{LHillier = "Hillier, L."}
@string{HHinssen = "Hinssen, Horst"}
@string{WHoff = "Hoff, Wouter D."}
@string{JLHolden = "Holden, J. L."}
@string{RAHolt = "Holt, R. A."}
+@string{MHonda = "Honda, M."}
@string{XHong = "Hong, Xia"}
@string{LHood = "Hood, L."}
@string{JHoover = "Hoover, J."}
@string{SImprota = "Improta, S."}
@string{TInoue = "Inoue, Tadashi"}
@string{IJBMM = "International Journal of Biological Macromolecules"}
+@string{HItoh = "Itoh, Hiroyasu"}
@string{AIrback = "Irback, Anders"}
@string{BIsralewitz = "Isralewitz, B."}
@string{SIstrail = "Istrail, S."}
@string{JACS = "Journal of the American Chemical Society"}
@string{JBM = "J Biomech"}
@string{JBT = "J Biotechnol"}
+@string{JEChem = "Journal of Electroanalytical Chemistry"}
@string{JMathBiol = "J Math Biol"}
+@string{JStructBiol = "Journal of structural biology"}
@string{JTB = "J Theor Biol"}
@string{WJang = "Jang, W."}
@string{LJanosi = "Janosi, Lorant"}
@string{RRJi = "Ji, R. R."}
@string{YJia = "Jia, Yiwei"}
@string{SJiang = "Jiang, Shaoyi"}
+@string{XJiang = "Jiang, Xingqun"}
@string{DJohannsmann = "Johannsmann, Diethelm"}
@string{CJohnson = "Johnson, Colin P."}
@string{JJohnson = "Johnson, J."}
@string{JCompP = "Journal of Computational Physics"}
@string{JMB = "Journal of Molecular Biology"}
@string{JP:CM = "Journal of Physics: Condensed Matter"}
+@string{JP:CON = "Journal of Physics: Conference Series"}
@string{JASA = "Journal of the American Statistical Association"}
@string{DAJuckett = "Juckett, D. A."}
@string{SRJun = "Jun, Se-Ran"}
@string{KKawasaki = "Kawasaki, K."}
@string{ZKe = "Ke, Z."}
@string{AKejariwal = "Kejariwal, A."}
-@string{MKellermayer = "Kellermayer, M."}
-@string{MSKellermayer = "Kellermayer, M. S."}
-@string{MSZKellermayer = "Kellermayer, Mikl\'os S. Z."}
+@string{MSKellermayer = "Kellermayer, Mikl\'os S. Z."}
+@string{TKempe = "Kempe, Thomas"}
@string{SKennedy = "Kennedy, S."}
+@string{SBHKent = "Kent, Stephen B. H."}
@string{WJKent = "Kent, W. J."}
@string{KAKetchum = "Ketchum, K. A."}
@string{FKienberger = "Kienberger, Ferry"}
@string{SHKim = "Kim, Sung-Hou"}
@string{WKing = "King, William Trevor"}
+@string{KKinosita = "{Kinosita Jr.}, Kazuhiko"}
@string{IRKirsch = "Kirsch, I. R."}
@string{JKlafter = "Klafter, J."}
@string{AKleiner = "Kleiner, Ariel"}
@string{ALevitsky = "Levitsky, A."}
@string{SLevy = "Levy, S."}
@string{MLewis = "Lewis, M."}
+@string{JLItalien = "L'Italien, James J."}
@string{BLi = "Li, Bing"}
@string{CYLi = "Li, Christopher Y."}
@string{HLi = "Li, Hongbin"}
@string{JLin = "Lin, Jianhua"}
@string{SHLin = "Lin, Sheng-Hsien"}
@string{XLin = "Lin, X."}
+@string{JLindahl = "Lindahl, Joakim"}
@string{WALinke = "Linke, Wolfgang A."}
@string{RLippert = "Lippert, R."}
@string{JLis = "Lis, John T."}
@string{WLiu = "Liu, W."}
@string{XLiu = "Liu, X."}
@string{YLiu = "Liu, Yichun"}
+@string{YSLo = "Lo, Yu-Shiu"}
@string{GLois = "Lois, Gregg"}
@string{JLopez = "Lopez, J."}
@string{LANL = "Los Alamos National Laboratory"}
@string{FLu = "Lu, F."}
@string{HLu = "Lu, Hui"}
@string{QLu = "Lu, Qinghua"}
-@string{MLudwig = "Ludwig, M."}
+@string{MLudwig = "Ludwig, Markus"}
@string{ZPLuo = "Luo, Zong-Ping"}
@string{ZLuthey-Schulten = "Luthey-Schulten, Z."}
@string{EMunck = {M\"unck, E.}}
@string{DMa = "Ma, D."}
+@string{LMa = "Ma, Liang"}
@string{MMaaloum = "Maaloum, Mounir"}
@string{Macromol = "Macromolecules"}
@string{AMadan = "Madan, A."}
@string{EMandello = "Mandello, Enrico"}
@string{GManderson = "Manderson, Gavin"}
@string{FMann = "Mann, F."}
+@string{AMansson = "M{\aa}nsson, Alf"}
@string{ERMardis = "Mardis, E. R."}
@string{JMarion = "Marion, J."}
@string{JFMarko = "Marko, John F."}
@string{PJMohr = "Mohr, Peter J."}
@string{VMontana = "Montana, Vedrana"}
@string{LMontanaro = "Montanaro, Lucio"}
+@string{LMontelius = "Montelius, Lars"}
+@string{CMontemagno = "Montemagno, Carlo D."}
@string{KTMontgomery = "Montgomery, K. T."}
@string{HMMoore = "Moore, H. M."}
@string{MMorgan = "Morgan, Michael"}
@string{VMoy = "Moy, Vincent T."}
@string{SMukamel = "Mukamel, Shaul"}
@string{PMundel = "Mundel, P."}
+@string{EMuneyuki = "Muneyuki, Eiro"}
@string{RJMural = "Mural, R. J."}
@string{BMurphy = "Murphy, B."}
@string{SMurphy = "Murphy, S."}
@string{NNguyen = "Nguyen, N."}
@string{TNguyen = "Nguyen, T."}
@string{MNguyen-Duong = "Nguyen-Duong, M."}
+@string{INicholls = "Nicholls, Ian A."}
@string{SNie = "Nie, S."}
@string{MNodell = "Nodell, M."}
@string{AANoegel = "Noegel, Angelika A."}
+@string{HNoji = "Noji, Hiroyuki"}
@string{RNome = "Nome, Rene A."}
@string{NNowak = "Nowak, N."}
@string{ANoy = "Noy, Aleksandr"}
@string{PDOlmsted = "Olmsted, Peter D."}
@string{AOlsen = "Olsen, A."}
@string{SJOlshansky = "Olshansky, S. J."}
+@string{POmling = {Omlink, P{\"a}r}}
@string{JNOnuchic = "Onuchic, J. N."}
@string{YOono = "Oono, Y."}
@string{COpitz = "Optiz, Christiane A."}
@string{OPerisic = "Perisic, Ognjen"}
@string{CPeterson = "Peterson, Craig L."}
@string{MPeterson = "Peterson, M."}
+@string{SMPeterson = "Peterson, Susan M."}
@string{CPfannkoch = "Pfannkoch, C."}
@string{PA = "Pflugers Arch"}
@string{PTRSL = "Philosophical Transactions of the Royal Society of London"}
@string{PRL = "Phys Rev Lett"}
@string{Physica = "Physica"}
@string{GPing = "Ping, Guanghui"}
+@string{NPinotsis = "Pinotsis, Nikos"}
+@string{DPlunkett = "Plunkett, David"}
@string{PPodsiadlo = "Podsiadlo, Paul"}
@string{ASPolitou = "Politou, A. S."}
@string{APoustka = "Poustka, A."}
@string{GPratesi = "Pratesi, G."}
@string{EPratts = "Pratts, E."}
@string{WPress = "Press, W."}
-@string{PNAS = "Proceedings of the National Academy of Sciences USA"}
+@string{PNAS = "Proceedings of the National Academy of Sciences of the
+ United States of America"}
@string{PBPMB = "Progress in Biophysics and Molecular Biology"}
@string{PS = "Protein Science"}
@string{PROT = "Proteins"}
@string{SRogic = "Rogic, S."}
@string{MRoman = "Roman, Marisa"}
@string{DRomblad = "Romblad, D."}
-@string{RRos = "Ros, R."}
+@string{RRos = "Ros, Robert"}
@string{BRosenberg = "Rosenberg, B."}
+@string{JRosengren = "Rosengren, Jenny P."}
@string{ARosenthal = "Rosenthal, A."}
@string{ARoters = "Roters, Andreas"}
@string{WRowe = "Rowe, W."}
@string{BRuhfel = "Ruhfel, B."}
@string{DBRusch = "Rusch, D. B."}
@string{JPRyckaert = "Ryckaert, Jean-Paul"}
+@string{NSakaki = "Sakaki, Naoyoshi"}
@string{YSakaki = "Sakaki, Y."}
@string{SSalzberg = "Salzberg, S."}
@string{BSamori = "Samor{\`i}, Bruno"}
@string{BSchlegelberger = "Schlegelberger, B."}
@string{MSchleicher = "Schleicher, Michael"}
@string{MSchlierf = "Schlierf, Michael"}
+@string{JSchmidt = "Schmidt, Jacob J."}
+@string{LSchmitt = "Schmitt, Lutz"}
@string{JSchmutz = "Schmutz, J."}
@string{GSchuler = "Schuler, G."}
@string{GDSchuler = "Schuler, G. D."}
@string{RScott = "Scott, R."}
@string{USeifert = "Seifert, Udo"}
@string{MSekhon = "Sekhon, M."}
+@string{TSekiguchi = "Sekiguchi, T."}
@string{BSenger = "Senger, B."}
@string{PSeranski = "Seranski, P."}
@string{RSesboue = {Sesbo\"u\'e, R.}}
@string{JShillcock = "Shillcock, Julian"}
@string{AShimizu = "Shimizu, A."}
@string{NShimizu = "Shimizu, N."}
+@string{RShimoKon = "Shimo-Kon, Rieko"}
@string{AShintani = "Shintani, A."}
@string{BShue = "Shue, B."}
@string{RSiebert = "Siebert, R."}
@string{ESuh = "Suh, E."}
@string{JSun = "Sun, J."}
@string{YLSun = "Sun, Yu-Long"}
+@string{MSundberg = "Sundberg, Mark"}
+@string{WSundquist = "Sundquist, Wesley I."}
@string{KSurewicz = "Surewicz, Krystyna"}
@string{WKSurewicz = "Surewicz, Witold K."}
@string{GGSutton = "Sutton, G. G."}
@string{ASzabo = "Szabo, Attila"}
+@string{STagerud = "T{\aa}gerud, Sven"}
@string{PTabor = "Tabor, P."}
+@string{ATakahashi = "Takahashi, Akiri"}
@string{DTalaga = "Talaga, David S."}
@string{PTalkner = "Talkner, Peter"}
+@string{RTampe = "Tamp{\'e}, Robert"}
@string{JTang = "Tang, Jianyong"}
@string{BNTaylor = "Taylor, Barry N."}
@string{STeukolsky = "Teukolsky, S."}
@string{JCMTsibris = "Tsibris, J.C.M."}
@string{LTskhovrebova = "Tskhovrebova, Larissa"}
@string{RTurner = "Turner, R."}
+@string{AUlman = "Ulman, Abraham"}
@string{UltraMic = "Ultramicroscopy"}
@string{UIP:Urbana = "University of Illinois Press, Urbana"}
+@string{UTMB = "University of Texas Medical Branch"}
@string{MUrbakh = "Urbakh, M."}
@string{KJVanVliet = "Van Vliet, Krystyn J."}
@string{CVech = "Vech, C."}
@string{Williams = "Williams"}
@string{MWilliams = "Williams, M."}
@string{SWilliams = "Williams, S."}
+@strinf{MWilmanns = "Wilmanns, Matthias"}
@string{RKWilson = "Wilson, R. K."}
@string{SWilson = "Wilson, Scott"}
@string{SWindsor = "Windsor, S."}
@string{JXi = "Xi, Jun"}
@string{AXia = "Xia, A."}
@string{CXiao = "Xiao, C."}
+@string{SXiao = "Xiao, Senbo"}
@string{TYada = "Yada, T."}
@string{CYan = "Yan, C."}
@string{MYandell = "Yandell, M."}
@string{GYang = "Yang, Guoliang"}
@string{YYang = "Yang, Yao"}
@string{AYao = "Yao, A."}
+@string{RYasuda = "Yaduso, Ryohei"}
@string{JYe = "Ye, J."}
@string{RYeh = "Yeh, Richard C."}
@string{RYonescu = "Yonescu, R."}
@string{SYooseph = "Yooseph, S."}
+@string{MYoshida = "Yoshida, Masasuke"}
@string{WYu = "Yu, Weichang"}
@string{JMYuan = "Yuan, Jian-Min"}
@string{AZandieh = "Zandieh, A."}
@string{HXZhou = "Zhou, Huan-Xiang"}
@string{SZhu = "Zhu, S."}
@string{XZhu = "Zhu, X."}
+@string{YJZhu = "Zhu, Ying-Jie"}
@string{WZhuang = "Zhuang, Wei"}
@string{NZinder = "Zinder, N."}
@string{RCZinober = "Zinober, Rebecca C."}
later."
}
+@article{ berkemeier11,
+ author = FBerkemeier #" and "# MBertz #" and "# SXiao #" and "#
+ NPinotsis #" and "# MWilmanns #" and "# FGrater #" and "# MRief,
+ title = "Fast-folding $\alpha$-helices as reversible strain absorbers
+ in the muscle protein myomesin.",
+ journal = PNAS,
+ year = 2011,
+ month = aug,
+ day = 23,
+ address = "Physik Department E22, Technische Universit{\"a}t
+ M{\"u}nchen, James-Franck-Stra{\ss}e, 85748 Garching, Germany.",
+ volume = 108,
+ number = 34,
+ pages = "14139--14144",
+ keywords = "Biomechanics",
+ keywords = "Kinetics",
+ keywords = "Microscopy, Atomic Force",
+ keywords = "Molecular Dynamics Simulation",
+ keywords = "Muscle Proteins",
+ keywords = "Protein Folding",
+ keywords = "Protein Multimerization",
+ keywords = "Protein Stability",
+ keywords = "Protein Structure, Secondary",
+ keywords = "Protein Structure, Tertiary",
+ keywords = "Protein Unfolding",
+ abstract = "The highly oriented filamentous protein network of
+ muscle constantly experiences significant mechanical load during
+ muscle operation. The dimeric protein myomesin has been identified
+ as an important M-band component supporting the mechanical
+ integrity of the entire sarcomere. Recent structural studies have
+ revealed a long $\alpha$-helical linker between the C-terminal
+ immunoglobulin (Ig) domains My12 and My13 of myomesin. In this
+ paper, we have used single-molecule force spectroscopy in
+ combination with molecular dynamics simulations to characterize
+ the mechanics of the myomesin dimer comprising immunoglobulin
+ domains My12-My13. We find that at forces of approximately 30?pN
+ the $\alpha$-helical linker reversibly elongates allowing the
+ molecule to extend by more than the folded extension of a full
+ domain. High-resolution measurements directly reveal the
+ equilibrium folding/unfolding kinetics of the individual helix. We
+ show that $\alpha$-helix unfolding mechanically protects the
+ molecule homodimerization from dissociation at physiologically
+ relevant forces. As fast and reversible molecular springs the
+ myomesin $\alpha$-helical linkers are an essential component for
+ the structural integrity of the M band.",
+ ISSN = "1091-6490",
+ doi = "10.1073/pnas.1105734108",
+ URL = "http://www.ncbi.nlm.nih.gov/pubmed/21825161",
+ language = "eng",
+}
+
@article { dill97,
author = KADill #" and "# HSChan,
title = "From Levinthal to pathways to funnels.",
}
@article { granzier97,
- author = HLGranzier #" and "# MKellermayer #" and "# MHelmes #" and "#
+ author = HLGranzier #" and "# MSKellermayer #" and "# MHelmes #" and "#
KTrombitas,
title = "Titin elasticity and mechanism of passive force development in rat
cardiac myocytes probed by thin-filament extraction",
}
@article { kellermayer03,
- author = MSZKellermayer #" and "# CBustamante #" and "# HLGranzier,
+ author = MSKellermayer #" and "# CBustamante #" and "# HLGranzier,
title = "Mechanics and structure of titin oligomers explored with atomic
force microscopy",
year = 2003,
between theory and rupture data from several different experiments."
}
+@article{ bartels03,
+ author = FWBartels #" and "# BBaumgarth #" and "# DAnselmetti
+ #" and "# RRos #" and "# ABecker,
+ title = "Specific binding of the regulatory protein Exp{G} to
+ promoter regions of the galactoglucan biosynthesis gene cluster of
+ Sinorhizobium meliloti--a combined molecular biology and force
+ spectroscopy investigation.",
+ journal = JStructBiol,
+ year = 2003,
+ month = aug,
+ address = "Experimentelle Biophysik, Fakult{\"a}t f{\"u}r Physik,
+ Universit{\"a}t Bielefeld, 33615 Bielefeld, Germany.",
+ volume = 143,
+ number = 2,
+ pages = "145--152",
+ keywords = "Base Sequence",
+ keywords = "Binding Sites",
+ keywords = "Conserved Sequence",
+ keywords = "Fungal Proteins",
+ keywords = "Galactans",
+ keywords = "Glucans",
+ keywords = "Kinetics",
+ keywords = "Microscopy, Atomic Force",
+ keywords = "Multigene Family",
+ keywords = "Polysaccharides, Bacterial",
+ keywords = "Promoter Regions, Genetic",
+ keywords = "Protein Binding",
+ keywords = "Sinorhizobium meliloti",
+ keywords = "Trans-Activators",
+ abstract = "Specific protein-DNA interaction is fundamental for all
+ aspects of gene transcription. We focus on a regulatory
+ DNA-binding protein in the Gram-negative soil bacterium
+ Sinorhizobium meliloti 2011, which is capable of fixing molecular
+ nitrogen in a symbiotic interaction with alfalfa plants. The ExpG
+ protein plays a central role in regulation of the biosynthesis of
+ the exopolysaccharide galactoglucan, which promotes the
+ establishment of symbiosis. ExpG is a transcriptional activator of
+ exp gene expression. We investigated the molecular mechanism of
+ binding of ExpG to three associated target sequences in the exp
+ gene cluster with standard biochemical methods and single molecule
+ force spectroscopy based on the atomic force microscope
+ (AFM). Binding of ExpG to expA1, expG-expD1, and expE1 promoter
+ fragments in a sequence specific manner was demonstrated, and a 28
+ bp conserved region was found. AFM force spectroscopy experiments
+ confirmed the specific binding of ExpG to the promoter regions,
+ with unbinding forces ranging from 50 to 165 pN in a logarithmic
+ dependence from the loading rates of 70-79000 pN/s. Two different
+ regimes of loading rate-dependent behaviour were
+ identified. Thermal off-rates in the range of k(off)=(1.2+/-1.0) x
+ 10(-3)s(-1) were derived from the lower loading rate regime for
+ all promoter regions. In the upper loading rate regime, however,
+ these fragments exhibited distinct differences which are
+ attributed to the molecular binding mechanism.",
+ ISSN = "1047-8477",
+ URL = "http://www.ncbi.nlm.nih.gov/pubmed/12972351",
+ language = "eng",
+}
+
@article { rief02,
author = MRief #" and "# HGrubmuller,
title = "Force spectroscopy of single biomolecules",
to be 20 +/- 3 pN and for A-T to be 9 +/- 3 pN."
}
+@article{ schmitt00,
+ author = LSchmitt #" and "# MLudwig #" and "# HEGaub #" and "# RTampe,
+ title = "A metal-chelating microscopy tip as a new toolbox for
+ single-molecule experiments by atomic force microscopy.",
+ journal = BPJ,
+ year = 2000,
+ month = jun,
+ address = "Institut f{\"u}r Physiologische Chemie,
+ Philipps-Universit{\"a}t Marburg, 35033 Marburg,
+ Germany. schmittl@mailer.uni-marburg.de",
+ volume = 78,
+ number = 6,
+ pages = "3275--3285",
+ keywords = "Chelating Agents",
+ keywords = "Edetic Acid",
+ keywords = "Histidine",
+ keywords = "Metals",
+ keywords = "Microscopy, Atomic Force",
+ keywords = "Nitrilotriacetic Acid",
+ keywords = "Peptides",
+ keywords = "Recombinant Fusion Proteins",
+ abstract = "In recent years, the atomic force microscope (AFM) has
+ contributed much to our understanding of the molecular forces
+ involved in various high-affinity receptor-ligand
+ systems. However, a universal anchor system for such measurements
+ is still required. This would open up new possibilities for the
+ study of biological recognition processes and for the
+ establishment of high-throughput screening applications. One such
+ candidate is the N-nitrilo-triacetic acid (NTA)/His-tag system,
+ which is widely used in molecular biology to isolate and purify
+ histidine-tagged fusion proteins. Here the histidine tag acts as a
+ high-affinity recognition site for the NTA chelator. Accordingly,
+ we have investigated the possibility of using this approach in
+ single-molecule force measurements. Using a histidine-peptide as a
+ model system, we have determined the binding force for various
+ metal ions. At a loading rate of 0.5 microm/s, the determined
+ forces varied from 22 +/- 4 to 58 +/- 5 pN. Most importantly, no
+ interaction was detected for Ca(2+) and Mg(2+) up to
+ concentrations of 10 mM. Furthermore, EDTA and a metal ion
+ reloading step demonstrated the reversibility of the
+ approach. Here the molecular interactions were turned off (EDTA)
+ and on (metal reloading) in a switch-like fashion. Our results
+ show that the NTA/His-tag system will expand the ``molecular
+ toolboxes'' with which receptor-ligand systems can be investigated
+ at the single-molecule level.",
+ ISSN = "0006-3495",
+ doi = "10.1016/S0006-3495(00)76863-9",
+ URL = "http://www.ncbi.nlm.nih.gov/pubmed/10828003",
+ language = "eng",
+}
+
@article { roters96,
author = ARoters #" and "# DJohannsmann,
title = "Distance-dependent noise measurements in scanning force
URL = "http://www.ncbi.nlm.nih.gov/pubmed/19336443",
language = "eng",
}
+
+@article{ kempe85,
+ author = TKempe #" and "# SBHKent #" and "# FChow #" and "# SMPeterson
+ #" and "# WSundquist #" and "# JLItalien #" and "# DHarbrecht
+ #" and "# DPlunkett #" and "# WDeLorbe,
+ title = "Multiple-copy genes: production and modification of
+ monomeric peptides from large multimeric fusion proteins.",
+ journal = GENE,
+ year = 1985,
+ volume = 39,
+ number = "2-3",
+ pages = "239--245",
+ keywords = "Cloning, Molecular",
+ keywords = "Cyanogen Bromide",
+ keywords = "DNA, Recombinant",
+ keywords = "Escherichia coli",
+ keywords = "Gene Expression Regulation",
+ keywords = "Genetic Vectors",
+ keywords = "Humans",
+ keywords = "Molecular Weight",
+ keywords = "Peptide Fragments",
+ keywords = "Plasmids",
+ keywords = "Substance P",
+ keywords = "beta-Galactosidase",
+ abstract = "A vector system has been designed for obtaining high
+ yields of polypeptides synthesized in Escherichia coli. Multiple
+ copies of a synthetic gene encoding the neuropeptide substance P
+ (SP) (Arg-Pro-Lys-Pro-Gln-Gln-Phe-Phe-Gly-Leu-Met-NH2) have been
+ linked and fused to the lacZ gene. Each copy of the SP gene was
+ flanked by codons for methionine to create sites for cleavage by
+ cyanogen bromide (CNBr). The isolated multimeric SP fusion
+ protein was converted to monomers of SP analog, each containing a
+ carboxyl-terminal homoserine lactone (Hse-lactone) residue
+ (Arg-Pro-Lys-Pro-Gln-Gln-Phe-Phe-Gly-Leu-Hse-lactone), upon
+ treatment with CNBr in formic acid. The Hse-lactone moiety was
+ subjected to chemical modifications to produce an SP Hse
+ amide. This method permits synthesis of peptide amide analogs and
+ other peptide derivatives by combining recombinant DNA techniques
+ and chemical methods.",
+ ISSN = "0378-1119",
+ URL = "http://www.ncbi.nlm.nih.gov/pubmed/2419204",
+ language = "eng",
+}
+
+@article{ honda08
+ author = MHonda #" and "# YBaba #" and "# NHiaro #" and "# TSekiguchi,
+ title = "Metal-molecular interface of sulfur-containing amino acid
+ and thiophene on gold surface",
+ journal = JP:CON,
+ volume = 100,
+ number = 5,
+ pages = "052071",
+ url = "http://dx.doi.org/10.1088/1742-6596/100/5/052071",
+ year = 2008,
+ abstract = "Chemical-bonding states of metal-molecular interface
+ have been investigated for L-cysteine and thiophene on gold by
+ x-ray photoelectron spectroscopy (XPS) and near edge x-ray
+ adsorption fine structure (NEXAFS). A remarkable difference in
+ Au-S bonding states was found between L-cysteine and
+ thiophene. For mono-layered L-cysteine on gold, the binding energy
+ of S 1s in XPS and the resonance energy at the S K-edge in NEXAFS
+ are higher by 8–9 eV than those for multi-layered film (molecular
+ L-cysteine). In contrast, the S K-edge resonance energy for
+ mono-layered thiophene on gold was 2475.0 eV, which is the same as
+ that for molecular L-cysteine. In S 1s XPS for mono-layered
+ thiophene, two peaks were observed. The higher binging-energy and
+ more intense peak at 2473.4 eV are identified as gold sulfide. The
+ binding energy of smaller peak, whose intensity is less than 1/3
+ of the higher binding energy peak, is 2472.2 eV, which is the same
+ as that for molecular thiophene. These observations indicate that
+ Au-S interface behavior shows characteristic chemical bond only
+ for the Au-S interface of L-cysteine monolayer on gold
+ substrate.",
+}
+
+@article{ ulman96,
+ author = AUlman,
+ title = "Formation and Structure of Self-Assembled Monolayers.",
+ journal = CHEMREV,
+ year = 1996,
+ month = jun,
+ day = 20,
+ address = "Department of Chemical Engineering, Chemistry and
+ Materials Science, and the Herman F. Mark Polymer Research
+ Institute, Polytechnic University, Six MetroTech Center, Brooklyn,
+ New York 11201.",
+ volume = 96,
+ number = 4,
+ pages = "1533--1554",
+ ISSN = "1520-6890",
+ URL = "http://www.ncbi.nlm.nih.gov/pubmed/11848802",
+ language = "eng",
+}
+
+@article{ hager02
+ author = GHager #" and "# ABrolo,
+ title = "Adsorption/desorption behaviour of cysteine and cystine in
+ neutral and basic media: electrochemical evidence for differing
+ thiol and disulfide adsorption to a {Au(111)} single crystal
+ electrode",
+ journal = JEChem,
+ volume = "550--551",
+ number = 0,
+ pages = "291--301",
+ year = 2003,
+ issn = "1572-6657",
+ doi = "10.1016/S0022-0728(03)00052-4",
+ url = "http://www.sciencedirect.com/science/article/pii/S0022072803000524",
+ keywords = "Thiol",
+ keywords = "Disulfide",
+ keywords = "Thiol adsorption",
+ keywords = "Self-assembled monolayers",
+ keywords = "Au(111) single crystal electrode",
+ keywords = "Cysteine",
+ keywords = "Cystine",
+ abstract = "The adsorption/desorption behaviour of the
+ thiol/disulfide redox couple, cysteine/cystine, was monitored at a
+ Au(111) single crystal electrode. The monolayers were formed
+ electrochemically from 0.1 M KClO4 and 0.1 M NaOH solutions
+ containing either the thiol or the disulfide. Distinct features in
+ the adsorption potential were noted. An adsorption peak was
+ observed in the cyclic voltammograms (CVs) from Au(111) in 0.1 M
+ KClO4 solutions containing cystine at $-0.57$ V vs. saturated
+ calomel electrode. Under the same conditions, the CVs from
+ solutions containing cysteine showed an adsorption peak at $-0.43$
+ V (0.14 V more positive than the corresponding peak from disulfide
+ solutions). This showed that the thiol and disulfide species have
+ different adsorption properties. Similar behaviour was observed in
+ 0.1 M NaOH. Cyclic voltammetric and chronocoulometric data were
+ employed to determine the surface coverage of the different
+ monolayers. Cysteine solutions prepared in 0.1 M KClO4 provided
+ coverages of $3.0\times10^{-10}$ and $2.5\times10^{-10}$
+ mol~cm$^{-2}$ for the L and the D--L species, respectively as
+ evaluated from the desorption peaks. Desorption of cystine in the
+ same medium yielded coverages of $1.2\times10^{-10}$ mol~cm$^{-2}$
+ for both L and D--L solutions (or $2.4\times10^{-10}$
+ mol~cm$^{-2}$ in cysteine equivalents). Surface coverages obtained
+ from Au(111) in 0.1 M NaOH corresponded to $3.9\times10^{10}$
+ mol~cm$^{-2}$ for L-cysteine, and $1.2\times10^{-10}$
+ mol~cm$^{-2}$ (or $2.4\times10^{-10}$ mol~cm$^{-2}$ cysteine
+ equivalents) for L and D--L cystine.",
+}
+
+@phdthesis{ ma10,
+ author = LMa,
+ title = "The Nanomechanics of Polycystin-1: A Kidney Mechanosensor",
+ school = UTMB,
+ year = 2010,
+ month = aug,
+ url = "http://etd.utmb.edu/theses/available/etd-07072010-132038/",
+ keywords = "ADPKD",
+ keywords = "Polycystin-1",
+ keywords = "Missense mutations",
+ keywords = "Atomic Force Microscopy",
+ keywords = "Osmolyte",
+ keywords = "Mechanosensor",
+ abstract = "Mutations in polycystin-1 (PC1) can cause Autosomal
+ Dominant Polycystic Kidney Disease (ADPKD), which is a leading
+ cause of renal failure. The available evidence suggests that PC1
+ acts as a mechanosensor, receiving signals from the primary cilia,
+ neighboring cells, and extracellular matrix. PC1 is a large
+ membrane protein that has a long N-terminal extracellular region
+ (about 3000 aa) with a multimodular structure including sixteen
+ Ig-like PKD domains, which are targeted by many naturally
+ occurring missense mutations. Nothing is known about the effects
+ of these mutations on the biophysical properties of PKD
+ domains. In addition, PC1 is expressed along the renal tubule,
+ where it is exposed to a wide range of concentration of urea. Urea
+ is known to destabilize proteins. Other osmolytes found in the
+ kidney such as sorbitol, betaine and TMAO are known to counteract
+ urea's negative effects on proteins. Nothing is known about how
+ the mechanical properties of PC1 are affected by these
+ osmolytes. Here I use nano-mechanical techniques to study the
+ effects of missense mutations and effects of denaturants and
+ various osmolytes on the mechanical properties of PKD
+ domains. Several missense mutations were found to alter the
+ mechanical stability of PKD domains resulting in distinct
+ mechanical phenotypes. Based on these findings, I hypothesize that
+ missense mutations may cause ADPKD by altering the stability of
+ the PC1 ectodomain, thereby perturbing its ability to sense
+ mechanical signals. I also found that urea has a significant
+ impact on both the mechanical stability and refolding rate of PKD
+ domains. It not only lowers their mechanical stability, but also
+ slows down their refolding rate. Moreover, several osmolytes were
+ found to effectively counteract the effects of urea. Our data
+ provide the evidence that naturally occurring osmolytes can help
+ to maintain Polycystin-1 mechanical stability and folding
+ kinetics. This study has the potential to provide new therapeutic
+ approaches (e.g. through the use of osmolytes or chemical
+ chaperones) for rescuing destabilized and misfolded PKD domains.",
+ language = "eng",
+}
+
+@article{ sundberg03,
+ author = MSundberg #" and "# JRosengren #" and "# RBunk
+ #" and "# JLindahl #" and "# INicholls #" and "# STagerud
+ #" and "# POmling #" and "# LMontelius #" and "# AMansson,
+ title = "Silanized surfaces for in vitro studies of actomyosin
+ function and nanotechnology applications.",
+ journal = ABioChem,
+ year = 2003,
+ month = dec,
+ day = 01,
+ address = "Department of Chemistry and Biomedical Sciences,
+ University of Kalmar, SE-391 82 Kalmar, Sweden.",
+ volume = 323,
+ number = 1,
+ pages = "127--138",
+ keywords = "Actomyosin",
+ keywords = "Adsorption",
+ keywords = "Animals",
+ keywords = "Collodion",
+ keywords = "Kinetics",
+ keywords = "Methods",
+ keywords = "Movement",
+ keywords = "Nanotechnology",
+ keywords = "Rabbits",
+ keywords = "Silicon",
+ keywords = "Surface Properties",
+ keywords = "Trimethylsilyl Compounds",
+ abstract = "We have previously shown that selective heavy meromyosin
+ (HMM) adsorption to predefined regions of nanostructured polymer
+ resist surfaces may be used to produce a nanostructured in vitro
+ motility assay. However, actomyosin function was of lower quality
+ than on conventional nitrocellulose films. We have therefore
+ studied actomyosin function on differently derivatized glass
+ surfaces with the aim to find a substitute for the polymer
+ resists. We have found that surfaces derivatized with
+ trimethylchlorosilane (TMCS) were superior to all other surfaces
+ tested, including nitrocellulose. High-quality actin filament
+ motility was observed up to 6 days after incubation with HMM and
+ the fraction of motile actin filaments and the velocity of smooth
+ sliding were generally higher on TMCS than on nitrocellulose. The
+ actomyosin function on TMCS-derivatized glass and nitrocellulose
+ is considered in relation to roughness and hydrophobicity of these
+ surfaces. The results suggest that TMCS is an ideal substitute for
+ polymer resists in the nanostructured in vitro motility
+ assay. Furthermore, TMCS derivatized glass also seems to offer
+ several advantages over nitrocellulose for HMM adsorption in the
+ ordinary in /vitro motility assay.",
+ ISSN = "0003-2697",
+ URL = "http://www.ncbi.nlm.nih.gov/pubmed/14622967",
+ doi = "10.1016/j.ab.2003.07.022",
+ language = "eng",
+}
+
+@article{ itoh04,
+ author = HItoh #" and "# ATakahashi #" and "# KAdachi #" and "#
+ HNoji #" and "# RYasuda #" and "# MYoshida #" and "#
+ KKinosita,
+ title = "Mechanically driven {ATP} synthesis by {F1}-{ATP}ase.",
+ journal = NAT,
+ year = 2004,
+ month = jan,
+ day = 29,
+ address = "Tsukuba Research Laboratory, Hamamatsu Photonics KK,
+ Joko, Hamamatsu 431-3103, Japan.
+ hiritoh@hpk.trc-net.co.jp",
+ volume = 427,
+ number = 6973,
+ pages = "465--468",
+ keywords = "Adenosine Diphosphate",
+ keywords = "Adenosine Triphosphate",
+ keywords = "Bacillus",
+ keywords = "Catalysis",
+ keywords = "Glass",
+ keywords = "Magnetics",
+ keywords = "Microchemistry",
+ keywords = "Microspheres",
+ keywords = "Molecular Motor Proteins",
+ keywords = "Proton-Translocating ATPases",
+ keywords = "Rotation",
+ keywords = "Torque",
+ abstract = "ATP, the main biological energy currency, is synthesized
+ from ADP and inorganic phosphate by ATP synthase in an
+ energy-requiring reaction. The F1 portion of ATP synthase, also
+ known as F1-ATPase, functions as a rotary molecular motor: in
+ vitro its gamma-subunit rotates against the surrounding
+ alpha3beta3 subunits, hydrolysing ATP in three separate catalytic
+ sites on the beta-subunits. It is widely believed that reverse
+ rotation of the gamma-subunit, driven by proton flow through the
+ associated F(o) portion of ATP synthase, leads to ATP synthesis in
+ biological systems. Here we present direct evidence for the
+ chemical synthesis of ATP driven by mechanical energy. We attached
+ a magnetic bead to the gamma-subunit of isolated F1 on a glass
+ surface, and rotated the bead using electrical magnets. Rotation
+ in the appropriate direction resulted in the appearance of ATP in
+ the medium as detected by the luciferase-luciferin reaction. This
+ shows that a vectorial force (torque) working at one particular
+ point on a protein machine can influence a chemical reaction
+ occurring in physically remote catalytic sites, driving the
+ reaction far from equilibrium.",
+ ISSN = "1476-4687",
+ doi = "10.1038/nature02212",
+ URL = "http://www.ncbi.nlm.nih.gov/pubmed/14749837",
+ language = "eng",
+}
+
+@article{ sakaki05,
+ author = NSakaki #" and "# RShimoKon #" and "# KAdachi
+ #" and "# HItoh #" and "# SFuruike #" and "# EMuneyuki
+ #" and "# MYoshida #" and "# KKinosita,
+ title = "One rotary mechanism for {F1}-{ATP}ase over {ATP}
+ concentrations from millimolar down to nanomolar.",
+ journal = BPJ,
+ year = 2005,
+ month = mar,
+ day = 30,
+ address = "Department of Functional Molecular Science, The Graduate
+ University for Advanced Studies, Nishigonaka 38, Myodaiji, Okazaki
+ 444-8585, Japan.",
+ volume = 88,
+ number = 3,
+ pages = "2047--2056",
+ keywords = "Adenosine Triphosphate",
+ keywords = "Hydrolysis",
+ keywords = "Kinetics",
+ keywords = "Microchemistry",
+ keywords = "Molecular Motor Proteins",
+ keywords = "Nanostructures",
+ keywords = "Protein Binding",
+ keywords = "Protein Conformation",
+ keywords = "Proton-Translocating ATPases",
+ keywords = "Rotation",
+ keywords = "Torque",
+ abstract = "F(1)-ATPase is a rotary molecular motor in which the
+ central gamma-subunit rotates inside a cylinder made of
+ alpha(3)beta(3)-subunits. The rotation is driven by ATP hydrolysis
+ in three catalytic sites on the beta-subunits. How many of the
+ three catalytic sites are filled with a nucleotide during the
+ course of rotation is an important yet unsettled question. Here we
+ inquire whether F(1) rotates at extremely low ATP concentrations
+ where the site occupancy is expected to be low. We observed under
+ an optical microscope rotation of individual F(1) molecules that
+ carried a bead duplex on the gamma-subunit. Time-averaged rotation
+ rate was proportional to the ATP concentration down to 200 pM,
+ giving an apparent rate constant for ATP binding of 2 x 10(7)
+ M(-1)s(-1). A similar rate constant characterized bulk ATP
+ hydrolysis in solution, which obeyed a simple Michaelis-Menten
+ scheme between 6 mM and 60 nM ATP. F(1) produced the same torque
+ of approximately 40 pN.nm at 2 mM, 60 nM, and 2 nM ATP. These
+ results point to one rotary mechanism governing the entire range
+ of nanomolar to millimolar ATP, although a switchover between two
+ mechanisms cannot be dismissed. Below 1 nM ATP, we observed less
+ regular rotations, indicative of the appearance of another
+ reaction scheme.",
+ ISSN = "0006-3495",
+ doi = "10.1529/biophysj.104.054668",
+ URL = "http://www.ncbi.nlm.nih.gov/pubmed/15626703",
+ language = "eng",
+}
+
+@article{ schmidt02,
+ author = JSchmidt #" and "# XJiang #" and "# CMontemagno,
+ title = "Force Tolerances of Hybrid Nanodevices",
+ journal = NANO,
+ volume = 2,
+ number = 11,
+ pages = "1229--1233",
+ year = 2002,
+ doi = "10.1021/nl025773v",
+ URL = "http://pubs.acs.org/doi/abs/10.1021/nl025773v",
+ eprint = "http://pubs.acs.org/doi/pdf/10.1021/nl025773v",
+ abstract = "We have created hybrid devices consisting of nanoscale
+ fabricated inorganic components integrated with and powered by a
+ genetically engineered motor protein. We wish to increase the
+ assembly yield and lifetime of these devices through
+ identification, measurement, and improvement of weak internal
+ bonds. Using dynamic force spectroscopy, we have measured the bond
+ rupture force of (histidine)\textsubscript{6} on a number of
+ different surfaces as a function of loading rate. The bond sizes,
+ lifetimes, and energy barrier heights were derived from these
+ measurements. We compare the (His)\textsubscript{6}--nickel bonds
+ to other bonds composing the hybrid device and describe
+ preliminary measurements of the force tolerances of the protein
+ itself. Pathways for improvement of device longevity and
+ robustness are discussed.",
+}
+
+@article{ lo01,
+ author = YSLo #" and "# YJZhu #" and "# TBeebe,
+ title = "Loading-Rate Dependence of Individual Ligand−Receptor
+ Bond-Rupture Forces Studied by Atomic Force Microscopy",
+ journal = LANG,
+ volume = 17,
+ number = 12,
+ pages = "3741--3748",
+ year = 2001,
+ doi = "10.1021/la001569g",
+ URL = "http://pubs.acs.org/doi/abs/10.1021/la001569g",
+ eprint = "http://pubs.acs.org/doi/pdf/10.1021/la001569g",
+ abstract = "It is known that bond strength is a dynamic property
+ that is dependent upon the force loading rate applied during the
+ rupturing of a bond. For biotin--avidin and biotin--streptavidin
+ systems, dynamic force spectra, which are plots of bond strength
+ vs loge(loading rate), have been acquired in a recent biomembrane
+ force probe (BFP) study at force loading rates in the range
+ 0.05--60 000 pN/s. In the present study, the dynamic force spectrum
+ of the biotin--streptavidin bond strength in solution was extended
+ from loading rates of ∼104 to ∼107 pN/s with the atomic force
+ microscope (AFM). A Poisson statistical analysis method was
+ applied to extract the magnitude of individual bond-rupture forces
+ and nonspecific interactions from the AFM force--distance curve
+ measurements. The bond strengths were found to scale linearly with
+ the logarithm of the loading rate. The nonspecific interactions
+ also exhibited a linear dependence on the logarithm of loading
+ rate, although not increasing as rapidly as the specific
+ interactions. The dynamic force spectra acquired here with the AFM
+ combined well with BFP measurements by Merkel et al. The combined
+ spectrum exhibited two linear regimes, consistent with the view
+ that multiple energy barriers are present along the unbinding
+ coordinate of the biotin--streptavidin complex. This study
+ demonstrated that unbinding forces measured by different
+ techniques are in agreement and can be used together to obtain a
+ dynamic force spectrum covering 9 orders of magnitude in loading
+ rate.",
+ note = "These guys seem to be pretty thorough, give this one another read.",
+}
projects / thesis.git / commitdiff