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Volumn 20, Issue 6, 2007, Pages 495-501

Energy landscape roughness of the streptavidin-biotin interaction

Author keywords

Atomic force microscopy; Dynamic force spectroscopy; Energy landscape; Energy landscape roughness; Energy surface; Free energy; Streptavidin biotin; Temperature

Indexed keywords

BIOTIN; STREPTAVIDIN;

EID: 38349086420     PISSN: 09523499     EISSN: 10991352     Source Type: Journal    
DOI: 10.1002/jmr.841     Document Type: Conference Paper
Times cited : (79)

References (45)
  • 1
    • 0037022522 scopus 로고    scopus 로고
    • Correction of microrheological measurements of soft samples with atomic force microscopy for the hydrodynamic drag on the cantilever
    • Alcaraz J, Buscemi L, Puig-de-Morales M, Colchero J, Baro A, Navajas D. 2002. Correction of microrheological measurements of soft samples with atomic force microscopy for the hydrodynamic drag on the cantilever. Langmuir 18(3): 716-721.
    • (2002) Langmuir , vol.18 , Issue.3 , pp. 716-721
    • Alcaraz, J.1    Buscemi, L.2    Puig-de-Morales, M.3    Colchero, J.4    Baro, A.5    Navajas, D.6
  • 3
    • 0018101150 scopus 로고
    • Models for specific adhesion of cells to cells
    • Bell GI. 1978. Models for specific adhesion of cells to cells. Science 200(4342): 618-627.
    • (1978) Science , vol.200 , Issue.4342 , pp. 618-627
    • Bell, G.I.1
  • 4
    • 33645765218 scopus 로고    scopus 로고
    • Single-molecule force spectroscopy reveals signatures of glassy dynamics in the energy landscape of ubiquitin
    • Brujic J, Hermans RI, Walther KA, Fernandez JM. 2006. Single-molecule force spectroscopy reveals signatures of glassy dynamics in the energy landscape of ubiquitin. Nat. Phy. 2(4): 282-286.
    • (2006) Nat. Phy , vol.2 , Issue.4 , pp. 282-286
    • Brujic, J.1    Hermans, R.I.2    Walther, K.A.3    Fernandez, J.M.4
  • 5
    • 0029407434 scopus 로고
    • Molecular-origins of the slow streptavidin-biotin dissociation kinetics
    • Chilkoti A, Stayton PS. 1995. Molecular-origins of the slow streptavidin-biotin dissociation kinetics. J. Am. Chem. Soc. 117(43): 10622-10628.
    • (1995) J. Am. Chem. Soc , vol.117 , Issue.43 , pp. 10622-10628
    • Chilkoti, A.1    Stayton, P.S.2
  • 6
    • 0028910003 scopus 로고
    • Site-directed mutagenesis studies of the high-affinity streptavidin-biotin complex - contributions of tryptophan residue-79, residue-108, and residue-120
    • Chilkoti A, Tan PH, Stayton PS. 1995. Site-directed mutagenesis studies of the high-affinity streptavidin-biotin complex - contributions of tryptophan residue-79, residue-108, and residue-120. Proc. Nat. Acad. Sci. USA 92(5): 1754-1758.
    • (1995) Proc. Nat. Acad. Sci. USA , vol.92 , Issue.5 , pp. 1754-1758
    • Chilkoti, A.1    Tan, P.H.2    Stayton, P.S.3
  • 7
    • 1542375742 scopus 로고    scopus 로고
    • Effects of intermediate bound states in dynamic force spectroscopy
    • Derenyi I, Bartolo D, Ajdari A. 2004. Effects of intermediate bound states in dynamic force spectroscopy. Biophys. J. 86(3): 1263-1269.
    • (2004) Biophys. J , vol.86 , Issue.3 , pp. 1263-1269
    • Derenyi, I.1    Bartolo, D.2    Ajdari, A.3
  • 8
    • 0034979287 scopus 로고    scopus 로고
    • Probing the relation between force - Lifetime - and chemistry in single molecular bonds
    • Evans E. 2001. Probing the relation between force - Lifetime - and chemistry in single molecular bonds. Annu. Rev. Biophys. Biomol. Struct. 30: 105-128.
    • (2001) Annu. Rev. Biophys. Biomol. Struct , vol.30 , pp. 105-128
    • Evans, E.1
  • 9
    • 0031001349 scopus 로고    scopus 로고
    • Dynamic strength of molecular adhesion bonds
    • Evans E, Ritchie K. 1997. Dynamic strength of molecular adhesion bonds. Biophys. J. 72(4): 1541-1555.
    • (1997) Biophys. J , vol.72 , Issue.4 , pp. 1541-1555
    • Evans, E.1    Ritchie, K.2
  • 10
    • 0028309424 scopus 로고
    • Adhesion forces between individual ligand-receptor pairs
    • Florin EL, Moy VT, Gaub HE. 1994. Adhesion forces between individual ligand-receptor pairs. Science 264(5157): 415-417.
    • (1994) Science , vol.264 , Issue.5157 , pp. 415-417
    • Florin, E.L.1    Moy, V.T.2    Gaub, H.E.3
  • 11
    • 0026320866 scopus 로고
    • The energy landscapes and motions of proteins
    • Frauenfelder H, Sligar SG, Wolynes PG. 1991. The energy landscapes and motions of proteins. Science 254(5038): 1598-1603.
    • (1991) Science , vol.254 , Issue.5038 , pp. 1598-1603
    • Frauenfelder, H.1    Sligar, S.G.2    Wolynes, P.G.3
  • 13
    • 0032577315 scopus 로고    scopus 로고
    • Structural studies of binding site tryptophan mutants in the high-affinity streptavidin-biotin complex
    • Freitag S, Trong IL, Chilkoti A, Klumb LA, Stayton PS, Stenkamp RE. 1998. Structural studies of binding site tryptophan mutants in the high-affinity streptavidin-biotin complex. J. Mol. Biol. 279(1): 211-221.
    • (1998) J. Mol. Biol , vol.279 , Issue.1 , pp. 211-221
    • Freitag, S.1    Trong, I.L.2    Chilkoti, A.3    Klumb, L.A.4    Stayton, P.S.5    Stenkamp, R.E.6
  • 14
    • 0030059225 scopus 로고    scopus 로고
    • Ligand binding: Molecular mechanics calculation of the streptavidin biotin rupture force
    • Grubmuller H, Heymann B, Tavan P. 1996. Ligand binding: molecular mechanics calculation of the streptavidin biotin rupture force. Science 271(5251): 997-999.
    • (1996) Science , vol.271 , Issue.5251 , pp. 997-999
    • Grubmuller, H.1    Heymann, B.2    Tavan, P.3
  • 15
    • 0347193736 scopus 로고
    • Reaction-rate theory - 50 years after Kramers
    • Hanggi P, Talkner P, Borkovec M. 1990. Reaction-rate theory - 50 years after Kramers. Rev. Mod. Phys. 62(2): 251-341.
    • (1990) Rev. Mod. Phys , vol.62 , Issue.2 , pp. 251-341
    • Hanggi, P.1    Talkner, P.2    Borkovec, M.3
  • 16
    • 36449007442 scopus 로고
    • Calibration of atomic-force microscope tips
    • Hutter JL, Bechhoefer J. 1993. Calibration of atomic-force microscope tips. Rev. Sci. Instrum. 64(7): 1868-1873.
    • (1993) Rev. Sci. Instrum , vol.64 , Issue.7 , pp. 1868-1873
    • Hutter, J.L.1    Bechhoefer, J.2
  • 17
    • 0041335634 scopus 로고    scopus 로고
    • Can energy landscape roughness of proteins and RNA be measured by using mechanical unfolding experiments?
    • Hyeon CB, Thirumalai D. 2003. Can energy landscape roughness of proteins and RNA be measured by using mechanical unfolding experiments? Proc. Nat. Acad. Sci. USA 100(18): 10249-10253.
    • (2003) Proc. Nat. Acad. Sci. USA , vol.100 , Issue.18 , pp. 10249-10253
    • Hyeon, C.B.1    Thirumalai, D.2
  • 20
    • 33846264595 scopus 로고    scopus 로고
    • Transmembrane helices have rough energy surfaces
    • Janovjak H, Knaus H, Muller DJ. 2007. Transmembrane helices have rough energy surfaces. J. Am. Chem. Soc. 129(2): 246-247.
    • (2007) J. Am. Chem. Soc , vol.129 , Issue.2 , pp. 246-247
    • Janovjak, H.1    Knaus, H.2    Muller, D.J.3
  • 21
    • 34547275473 scopus 로고
    • Brownian motion in a field of force and the diffusion model of chemical reactions
    • Kramers HA. 1940. Brownian motion in a field of force and the diffusion model of chemical reactions. Physica 7(4): 304.
    • (1940) Physica , vol.7 , Issue.4 , pp. 304
    • Kramers, H.A.1
  • 22
    • 0028381539 scopus 로고
    • Sensing discrete streptavidin biotin interactions with atomic-force microscopy
    • Lee GU, Kidwell DA, Colton RJ. 1994. Sensing discrete streptavidin biotin interactions with atomic-force microscopy. Langmuir 10(2): 354-357.
    • (1994) Langmuir , vol.10 , Issue.2 , pp. 354-357
    • Lee, G.U.1    Kidwell, D.A.2    Colton, R.J.3
  • 23
    • 0037306230 scopus 로고    scopus 로고
    • Force measurements of the alpha(5)beta(1) integrin-fibronectin interaction
    • Li FY, Redick SD, Erickson HP, Moy VT. 2003. Force measurements of the alpha(5)beta(1) integrin-fibronectin interaction. Biophys. J. 84(2): 1252-1262.
    • (2003) Biophys. J , vol.84 , Issue.2 , pp. 1252-1262
    • Li, F.Y.1    Redick, S.D.2    Erickson, H.P.3    Moy, V.T.4
  • 25
    • 0033531109 scopus 로고    scopus 로고
    • Energy landscapes of receptor-ligand bonds explored with dynamic force spectroscopy
    • Merkel R, Nassoy P, Leung A, Ritchie K, Evans E. 1999. Energy landscapes of receptor-ligand bonds explored with dynamic force spectroscopy. Nature 397(6714): 50-53.
    • (1999) Nature , vol.397 , Issue.6714 , pp. 50-53
    • Merkel, R.1    Nassoy, P.2    Leung, A.3    Ritchie, K.4    Evans, E.5
  • 26
    • 0028140707 scopus 로고
    • Intermolecular forces and energies between ligands and receptors
    • Moy VT, Florin EL, Gaub. HE. 1994. Intermolecular forces and energies between ligands and receptors. Science 266(5183): 257-259.
    • (1994) Science , vol.266 , Issue.5183 , pp. 257-259
    • Moy, V.T.1    Florin, E.L.2    Gaub, H.E.3
  • 27
    • 30644476474 scopus 로고    scopus 로고
    • Dynamic force spectroscopy of the digoxigenin-antibody complex
    • Neuert G, Albrecht C, Pamir E, Gaub. HE. 2006. Dynamic force spectroscopy of the digoxigenin-antibody complex. FEBS Lett. 580(2): 505-509.
    • (2006) FEBS Lett , vol.580 , Issue.2 , pp. 505-509
    • Neuert, G.1    Albrecht, C.2    Pamir, E.3    Gaub, H.E.4
  • 28
    • 20044395620 scopus 로고    scopus 로고
    • Direct measurement of protein energy landscape roughness
    • Nevo R, Brumfeld V, Kapon R, Hinterdorfer P, Reich Z. 2005. Direct measurement of protein energy landscape roughness. EMBO Rep. 6(5): 482-486.
    • (2005) EMBO Rep , vol.6 , Issue.5 , pp. 482-486
    • Nevo, R.1    Brumfeld, V.2    Kapon, R.3    Hinterdorfer, P.4    Reich, Z.5
  • 29
    • 28444492383 scopus 로고    scopus 로고
    • The solution to the streptavidin-biotin paradox: The influence of history on the strength of single molecular bonds
    • Pincet F, Husson J. 2005. The solution to the streptavidin-biotin paradox: the influence of history on the strength of single molecular bonds. Biophys. J. 89(6): 4374-4381.
    • (2005) Biophys. J , vol.89 , Issue.6 , pp. 4374-4381
    • Pincet, F.1    Husson, J.2
  • 30
    • 31144451131 scopus 로고    scopus 로고
    • Reaction rate theory: What it was, where is it today, and where is it going?
    • Pollak E, Talkner P. 2005. Reaction rate theory: what it was, where is it today, and where is it going? Chaos 15(2): 26116.
    • (2005) Chaos , vol.15 , Issue.2 , pp. 26116
    • Pollak, E.1    Talkner, P.2
  • 31
    • 27644473726 scopus 로고    scopus 로고
    • Temperature softening of a protein in single-molecule experiments
    • Schlierf M, Rief M. 2005. Temperature softening of a protein in single-molecule experiments. J. Mol. Biol. 354(2): 497-503.
    • (2005) J. Mol. Biol , vol.354 , Issue.2 , pp. 497-503
    • Schlierf, M.1    Rief, M.2
  • 35
    • 0024588901 scopus 로고
    • Structural origins of high-affinity biotin binding to streptavidin
    • Weber PC, Ohlendorf DH, Wendoloski JJ, Salemme FR. 1989. Structural origins of high-affinity biotin binding to streptavidin. Science 243(4887): 85-88.
    • (1989) Science , vol.243 , Issue.4887 , pp. 85-88
    • Weber, P.C.1    Ohlendorf, D.H.2    Wendoloski, J.J.3    Salemme, F.R.4
  • 36
    • 0026606240 scopus 로고
    • Crystallographic and thermodynamic comparison of natural and synthetic ligands bound to streptavidin
    • Weber PC, Wendoloski JJ, Pantoliano MW, Salemme FR. 1992. Crystallographic and thermodynamic comparison of natural and synthetic ligands bound to streptavidin. J. Am. Chem. Soc. 114(9): 3197-3200.
    • (1992) J. Am. Chem. Soc , vol.114 , Issue.9 , pp. 3197-3200
    • Weber, P.C.1    Wendoloski, J.J.2    Pantoliano, M.W.3    Salemme, F.R.4
  • 37
    • 0000548761 scopus 로고
    • Crystallographic and thermodynamic comparison of structurally diverse molecules binding to streptavidin
    • Weber PC, Pantoliano MW, Salemme FR. 1995. Crystallographic and thermodynamic comparison of structurally diverse molecules binding to streptavidin. Acta Crystallogr. D Biol. Crystallogr. 51: 590-596.
    • (1995) Acta Crystallogr. D Biol. Crystallogr , vol.51 , pp. 590-596
    • Weber, P.C.1    Pantoliano, M.W.2    Salemme, F.R.3
  • 38
    • 33846006584 scopus 로고    scopus 로고
    • Force spectroscopy of LFA-1 and its ligands, ICAM-1 and ICAM-2
    • Wojcikiewicz EP, Abdulreda MH, Zhang X, Moy VT. 2006. Force spectroscopy of LFA-1 and its ligands, ICAM-1 and ICAM-2. Biomacromolecules 7(11): 3188-3195.
    • (2006) Biomacromolecules , vol.7 , Issue.11 , pp. 3188-3195
    • Wojcikiewicz, E.P.1    Abdulreda, M.H.2    Zhang, X.3    Moy, V.T.4
  • 39
    • 0033621525 scopus 로고    scopus 로고
    • Direct force measurements of the streptavidin-biotin interaction
    • Wang J, Chilkoti A, Moy VT. (1999). Direct force measurements of the streptavidin-biotin interaction. Biomolecular Engneering 16(1-4): 45-55.
    • (1999) Biomolecular Engneering , vol.16 , Issue.1-4 , pp. 45-55
    • Wang, J.1    Chilkoti, A.2    Moy, V.T.3
  • 40
    • 33846524439 scopus 로고    scopus 로고
    • Motifs for molecular recognition exploiting hydrophobic enclosure in protein-ligand binding
    • Young T, Abel R, Kim B, Berne BJ, Friesner RA. 2007. Motifs for molecular recognition exploiting hydrophobic enclosure in protein-ligand binding. Proc. Natl. Acad. Sci. USA 104(3): 808-813.
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , Issue.3 , pp. 808-813
    • Young, T.1    Abel, R.2    Kim, B.3    Berne, B.J.4    Friesner, R.A.5
  • 41
    • 0034702770 scopus 로고    scopus 로고
    • Energy landscape of streptavidin-biotin complexes measured by atomic force microscopy
    • Yuan C, Chen A, Kolb P, Moy VT. 2000. Energy landscape of streptavidin-biotin complexes measured by atomic force microscopy. Biochemistry 39(33): 10219-10223.
    • (2000) Biochemistry , vol.39 , Issue.33 , pp. 10219-10223
    • Yuan, C.1    Chen, A.2    Kolb, P.3    Moy, V.T.4
  • 42
    • 2442509841 scopus 로고    scopus 로고
    • Molecular basis of the dynamic strength of the sialyl Lewis X-selectin interaction
    • Zhang XH, Bogorin DF, Moy VT. 2004. Molecular basis of the dynamic strength of the sialyl Lewis X-selectin interaction. Chemphyschem 5(2): 175-182.
    • (2004) Chemphyschem , vol.5 , Issue.2 , pp. 175-182
    • Zhang, X.H.1    Bogorin, D.F.2    Moy, V.T.3
  • 43
    • 16344392756 scopus 로고    scopus 로고
    • Molecular basis for the dynamic strength of the integrin alpha(4)beta(1)/VCAM-1 interaction
    • Zhang XH, Craig SE, Kirby H, Humphries MJ, Moy VT. 2004. Molecular basis for the dynamic strength of the integrin alpha(4)beta(1)/VCAM-1 interaction. Biophys. J. 87(5): 3470-3478.
    • (2004) Biophys. J , vol.87 , Issue.5 , pp. 3470-3478
    • Zhang, X.H.1    Craig, S.E.2    Kirby, H.3    Humphries, M.J.4    Moy, V.T.5
  • 44
    • 33748698955 scopus 로고    scopus 로고
    • Unbinding of the streptavidin-biotin complex by atomic force microscopy: A hybrid simulation study
    • Zhou J, Zhang LZ, Leng YS, Tsao HK, Sheng YJ, Jiang SY. 2006. Unbinding of the streptavidin-biotin complex by atomic force microscopy: a hybrid simulation study. J. Chem. Phys. 125(10): 104905.
    • (2006) J. Chem. Phys , vol.125 , Issue.10 , pp. 104905
    • Zhou, J.1    Zhang, L.Z.2    Leng, Y.S.3    Tsao, H.K.4    Sheng, Y.J.5    Jiang, S.Y.6
  • 45
    • 0024121530 scopus 로고
    • Diffusion in a rough potential
    • Zwanzig R. 1988. Diffusion in a rough potential. Proc. Natl. Acad. Sci. USA 85(7): 2029-2030.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , Issue.7 , pp. 2029-2030
    • Zwanzig, R.1


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