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Volumn 99, Issue 1, 2010, Pages 323-332

Force-induced lysozyme-HyHEL5 antibody dissociation and its analysis by means of a cooperative binding model

Author keywords

[No Author keywords available]

Indexed keywords

ALANINE; ANTIBODY; LYSOZYME; PROTEIN BINDING;

EID: 77954318864     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1016/j.bpj.2010.03.060     Document Type: Article
Times cited : (9)

References (56)
  • 2
    • 0028007197 scopus 로고
    • Direct measurement of the forces between complementary strands of DNA
    • Lee, G. U., L. A. Chrisey, and R. J. Colton. 1994. Direct measurement of the forces between complementary strands of DNA. Science. 266:771-773.
    • (1994) Science. , vol.266 , pp. 771-773
    • Lee, G.U.1    Chrisey, L.A.2    Colton, R.J.3
  • 3
    • 0028140707 scopus 로고
    • Intermolecular forces and energies between ligands and receptors
    • Moy, V. T., E.-L. Florin, and H. E. Gaub. 1994. Intermolecular forces and energies between ligands and receptors. Science. 266:257-259. (Pubitemid 24343509)
    • (1994) Science , vol.266 , Issue.5183 , pp. 257-259
    • Moy, V.T.1    Florin, E.-L.2    Gaub, H.E.3
  • 4
    • 0031002460 scopus 로고    scopus 로고
    • Foldingunfolding transitions in single titin molecules characterized with laser tweezers
    • Kellermayer, M. S. Z., S. B. Smith, ..., C. Bustamante. 1997. Foldingunfolding transitions in single titin molecules characterized with laser tweezers. Science. 276:1112-1116.
    • (1997) Science. , vol.276 , pp. 1112-1116
    • Kellermayer, M.S.Z.1    Smith, S.B.2    Bustamante, C.3
  • 5
    • 0031011695 scopus 로고    scopus 로고
    • Reversible unfolding of individual titin immunoglobulin domains by AFM
    • DOI 10.1126/science.276.5315.1109
    • Rief, M., M. Gautel, ..., H. E. Gaub. 1997. Reversible unfolding of individual titin immunoglobulin domains by AFM. Science. 276: 1109-1112. (Pubitemid 27218118)
    • (1997) Science , vol.276 , Issue.5315 , pp. 1109-1112
    • Rief, M.1    Gautel, M.2    Oesterhelt, F.3    Fernandez, J.M.4    Gaub, H.E.5
  • 7
    • 4243754128 scopus 로고    scopus 로고
    • Nonequilibrium equality for free energy differences
    • Jarzynski, C. 1997. Nonequilibrium equality for free energy differences. Phys. Rev. Lett. 78:2690-2693. (Pubitemid 127655287)
    • (1997) Physical Review Letters , vol.78 , Issue.14 , pp. 2690-2693
    • Jarzynski, C.1
  • 9
    • 0037036070 scopus 로고    scopus 로고
    • Equilibrium information from nonequilibrium measurements in an experimental test of Jarzynski's equality
    • DOI 10.1126/science.1071152
    • Liphardt, J., S. Dumont, ..., C. Bustamante. 2002. Equilibrium information from nonequilibrium measurements in an experimental test of Jarzynski's equality. Science. 296:1832-1835. (Pubitemid 34596263)
    • (2002) Science , vol.296 , Issue.5574 , pp. 1832-1835
    • Liphardt, J.1    Dumont, S.2    Smith, S.B.3    Tinoco Jr., I.4    Bustamante, C.5
  • 10
    • 34547275473 scopus 로고
    • Brownian motion in a field of force and the diffusion model of chemical reactions
    • Kramers, H.A. 1940. Brownian motion in a field of force and the diffusion model of chemical reactions. Physica. 7:284-304.
    • (1940) Physica. , vol.7 , pp. 284-304
    • Kramers, H.A.1
  • 11
    • 0031001349 scopus 로고    scopus 로고
    • Dynamic strength of molecular adhesion bonds
    • Evans, E., and K. Ritchie. 1997. Dynamic strength of molecular adhesion bonds. Biophys. J. 72:1541-1555. (Pubitemid 27133095)
    • (1997) Biophysical Journal , vol.72 , Issue.4 , pp. 1541-1555
    • Evans, E.1    Ritchie, K.2
  • 13
    • 0034979287 scopus 로고    scopus 로고
    • Probing the relation between force - Lifetime - and chemistry in single molecular bonds
    • DOI 10.1146/annurev.biophys.30.1.105
    • Evans, E. 2001. Probing the relation between force-lifetime and chemistry in single molecular bonds. Annu. Rev. Biophys. Biomol. Struct. 30:105-128. (Pubitemid 32566158)
    • (2001) Annual Review of Biophysics and Biomolecular Structure , vol.30 , pp. 105-128
    • Evans, E.1
  • 14
    • 0030872242 scopus 로고    scopus 로고
    • Reconstructing potential energy functions from simulated force-induced unbinding processes
    • Balsera, M., S. Stepaniants, ..., K. Schulten. 1997. Reconstructing potential energy functions from simulated force-induced unbinding processes. Biophys. J. 73:1281-1287. (Pubitemid 27360718)
    • (1997) Biophysical Journal , vol.73 , Issue.3 , pp. 1281-1287
    • Balsera, M.1    Stepaniants, S.2    Izrailev, S.3    Oono, Y.4    Schulten, K.5
  • 15
    • 0033531109 scopus 로고    scopus 로고
    • Energy landscapes of receptor-ligand bonds explored with dynamic force spectroscopy
    • DOI 10.1038/16219
    • Merkel, R., P. Nassoy, ..., E. Evans. 1999. Energy landscapes of receptor-ligand bonds explored with dynamic force spectroscopy. Nature, 397:50-53. (Pubitemid 29038244)
    • (1999) Nature , vol.397 , Issue.6714 , pp. 50-53
    • Merkel, R.1    Nassoy, P.2    Leung, A.3    Ritchie, K.4    Evans, E.5
  • 16
    • 0033861876 scopus 로고    scopus 로고
    • Model energy landscapes and the force-induced dissociation of ligand-receptor bonds
    • Strunz, T., K. Oroszlan, ..., M. Hegner. 2000. Model energy landscapes and the force-induced dissociation of ligand-receptor bonds. Biophys. J. 79:1206-1212.
    • (2000) Biophys. J. , vol.79 , pp. 1206-1212
    • Strunz, T.1    Oroszlan, K.2    Hegner, M.3
  • 17
    • 0141816804 scopus 로고    scopus 로고
    • Beyond the conventional description of dynamic force spectroscopy of adhesion bonds
    • Dudko, O. K., A. E. Filippov, ..., M. Urbakh. 2003. Beyond the conventional description of dynamic force spectroscopy of adhesion bonds. Proc. Natl. Acad. Sci. USA. 100:11378-11381.
    • (2003) Proc. Natl. Acad. Sci. USA. , vol.100 , pp. 11378-11381
    • Dudko, O.K.1    Filippov, A.E.2    Urbakh, M.3
  • 18
    • 0038650860 scopus 로고    scopus 로고
    • Kinetics from nonequilibrium single-molecule pulling experiments
    • Hummer, G., and A. Szabo. 2003. Kinetics from nonequilibrium singlemoleculle pulling experiments. Biophys. J. 85:5-15. (Pubitemid 36753612)
    • (2003) Biophysical Journal , vol.85 , Issue.1 , pp. 5-15
    • Hummer, G.1    Szabo, A.2
  • 19
    • 33645004171 scopus 로고    scopus 로고
    • Intrinsic rates and activation free energies from single-molecule pulling experiments
    • Dudko, O. K., G. Hummer, and A. Szabo. 2006. Intrinsic rates and activation free energies from single-molecule pulling experiments. Phys. Rev. Lett. 96, 108191-1-4.
    • (2006) Phys. Rev. Lett. , vol.96 , pp. 1081911-1081914
    • Dudko, O.K.1    Hummer, G.2    Szabo, A.3
  • 22
    • 0034874258 scopus 로고    scopus 로고
    • Molecular dynamics force probe simulations of antibody/antigen unbinding: Entropic control and nonadditivity of unbinding forces
    • Heymann, B., and H. Grubmüller. 2001. Molecular dynamics force probe simulations of antibody/antigen unbinding: entropic control and nonadditivity of unbinding forces. Biophys. J. 81:1295-1313. (Pubitemid 32783574)
    • (2001) Biophysical Journal , vol.81 , Issue.3 , pp. 1295-1313
    • Heymann, B.1    Grubmuller, H.2
  • 23
    • 0030059225 scopus 로고    scopus 로고
    • Ligand binding: Molecular mechanics calculation of the streptavidin-biotin rupture force
    • Grubmüller, H., B. Heymann, and P. Tavan. 1996. Ligand binding: molecular mechanics calculation of the streptavidin-biotin rupture force. Science. 271:997-999. (Pubitemid 26066398)
    • (1996) Science , vol.271 , Issue.5251 , pp. 997-999
    • Grubmuller, H.1    Heymann, B.2    Tavan, P.3
  • 24
    • 0033578783 scopus 로고    scopus 로고
    • Salt links dominate affinity of antibody HyHEL-5 for lysozyme through enthalpic contributions
    • Wibbenmeyer, J. A., P. Schuck, ..., R. C. Willson. 1999. Salt links dominate affinity of antibody HyHEL-5 for lysozyme through enthalpic contributions. J. Biol. Chem. 274:26838-26842. (Pubitemid 129520203)
    • (1999) Journal of Biological Chemistry , vol.274 , Issue.38 , pp. 26838-26842
    • Wibbenmeyer, J.A.1    Schuck, P.2    Smith-Gill, S.J.3    Willson, R.C.4
  • 25
    • 77954317792 scopus 로고    scopus 로고
    • A statistical model for antibodyantigen binding
    • Katletz, S., and U. M. Titulaer. 1999. A statistical model for antibodyantigen binding. Cond. Matter Phys. 2:361-368.
    • (1999) Cond. Matter Phys. , vol.2 , pp. 361-368
    • Katletz, S.1    Titulaer, U.M.2
  • 26
    • 11644279337 scopus 로고
    • Time-dependent statistics of the ising model
    • Glauber, R. J. 1963. Time-dependent statistics of the Ising model. J. Math. Phys. 4:294-307.
    • (1963) J. Math. Phys. , vol.4 , pp. 294-307
    • Glauber, R.J.1
  • 27
    • 0015223587 scopus 로고
    • Co-operative non-enzymic base recognition. 3. Kinetics of the helix-coil transition of the oligoribouridylic-oligoriboadenylic acid system and of oligoriboadenylic acid alone at acidic pH
    • Pörschke, D., and M. Eigen. 1971. Co-operative non-enzymic base recognition. 3. Kinetics of the helix-coil transition of the oligoribouridylic-oligoriboadenylic acid system and of oligoriboadenylic acid alone at acidic pH. J. Mol. Biol. 62:361-381.
    • (1971) J. Mol. Biol. , vol.62 , pp. 361-381
    • Pörschke, D.1    Eigen, M.2
  • 28
    • 0000792867 scopus 로고
    • The application of the theory of stochastic processes to chemical kinetics
    • John Wiley, New York
    • Montroll, E. W., and K. E. Shuler. 1958. The application of the theory of stochastic processes to chemical kinetics. In Advances in Chemical. Physics., Vol, 1. John Wiley, New York.
    • (1958) Advances in Chemical. Physics. , vol.1
    • Montroll, E.W.1    Shuler, K.E.2
  • 29
    • 0012697813 scopus 로고
    • General co-operative kinetics on a linear ISING lattice
    • Schwarz, G. 1971, General co-operative kinetics on a linear ISING lattice. Ber. Bunsenges. Phys. Chem. 75:40-45.
    • (1971) Ber. Bunsenges. Phys. Chem. , vol.75 , pp. 40-45
    • Schwarz, G.1
  • 31
    • 36449007442 scopus 로고
    • Calibration of atomic-force microscope tips
    • Hutter, J. L., and J. Bechhoefer. 1993. Calibration of atomic-force microscope tips. Rev. Sci. Instrum. 64:1868-1873.
    • (1993) Rev. Sci. Instrum. , vol.64 , pp. 1868-1873
    • Hutter, J.L.1    Bechhoefer, J.2
  • 32
    • 34347209835 scopus 로고
    • Calculation of thermal noise in atomic force microscopy
    • Butt, H. J., and M. Jaschke. 1995. Calculation of thermal noise in atomic force microscopy. Nanotechnology. 6:1-7.
    • (1995) Nanotechnology. , vol.6 , pp. 1-7
    • Butt, H.J.1    Jaschke, M.2
  • 34
    • 0028381539 scopus 로고
    • Sensing discrete streptavidin-biotin interactions with atomic force microscopy
    • Lee, G. U., D. A. Kidwell, and R. J. Colton. 1994. Sensing discrete streptavidin-biotin interactions with atomic force microscopy. Langmut. 10:354-357.
    • (1994) Langmut. , vol.10 , pp. 354-357
    • Lee, G.U.1    Kidwell, D.A.2    Colton, R.J.3
  • 35
    • 0028309424 scopus 로고
    • Adhesion forces between individual ligand-receptor pairs
    • Florin, E.-L., V. T. Moy, and H. E. Gaub. 1994. Adhesion forces between individual ligand-receptor pairs. Science. 264:415-417.
    • (1994) Science. , vol.264 , pp. 415-417
    • Florin, E.-L.1    Moy, V.T.2    Gaub, H.E.3
  • 37
    • 0033973107 scopus 로고    scopus 로고
    • Data analysis of interaction forces measured with the atomic force microscope
    • DOI 10.1016/S0304-3991(99)00154-0, PII S0304399199001540
    • Baumgartner, W., P. Hinterdorfer, and H. Schindler. 2000. Data analysis of interaction forces measured with the atomic force microscope. Ultramicroscopy. 82:85-95. (Pubitemid 30070088)
    • (2000) Ultramicroscopy , vol.82 , Issue.1-4 , pp. 85-95
    • Baumgartner, W.1    Hinterdorfer, P.2    Schindler, H.3
  • 39
    • 0034730166 scopus 로고    scopus 로고
    • Unbinding forces of single antibody-antigen complexes correlate with their thermal dissociation rates
    • Schwesinger, F., R. Ros, ..., .A. Pluckthun. 2000. Unbinding forces of single antibody-antigen complexes correlate with their thermal dissociation rates. Proc. Natl. Acad. Sci. USA. 97:9972-9977.
    • (2000) Proc. Natl. Acad. Sci. USA. , vol.97 , pp. 9972-9977
    • Schwesinger, F.1    Ros, R.2    Pluckthun, A.3
  • 40
    • 0000414190 scopus 로고    scopus 로고
    • Static and dynamical properties of single poly(ethylene glycol) molecules investigated by force spectroscopy
    • Kienberger, F., V. P. Pastushenko, ..., P. Hinterdorfer. 2000. Static and dynamical properties of single poly(ethylene glycol) molecules investigated by force spectroscopy. Single Mol. 1:123-128.
    • (2000) Single Mol. , vol.1 , pp. 123-128
    • Kienberger, F.1    Pastushenko, V.P.2    Hinterdorfer, P.3
  • 42
    • 0028071373 scopus 로고
    • Entropic elasticity of A-phage DNA
    • Bustamante, C., J. F. Marko, ..., S. Smith, 1994. Entropic elasticity of A-phage DNA. Science. 265:1599-1600.
    • (1994) Science. , vol.265 , pp. 1599-1600
    • Bustamante, C.1    Marko, J.F.2    Smith, S.3
  • 43
    • 0032988663 scopus 로고    scopus 로고
    • Strength of a weak bond connecting flexible polymer chains
    • Evans, E., and K. Ritchie. 1999. Strength of a weak bond connecting flexible polymer chains. Biophys. J. 76:2439-2447. (Pubitemid 29264606)
    • (1999) Biophysical Journal , vol.76 , Issue.5 , pp. 2439-2447
    • Evans, E.A.1    Ritchie, K.2
  • 44
    • 0032869084 scopus 로고    scopus 로고
    • Antibody recognition imaging by atomic force microscopy
    • Raab, A., W. Han, ..., P. Hinterdorfer. 1997. Antibody recognition imaging by atomic force microscopy. Nat. Biotechnol. 17:902-905.
    • (1997) Nat. Biotechnol. , vol.17 , pp. 902-905
    • Raab, A.1    Han, W.2    Hinterdorfer, P.3
  • 45
    • 0018101150 scopus 로고
    • Models for the specific adhesion of cells to cells
    • Bell, G. I. 1978. Models for the specific adhesion of cells to cells. Science, 200:618-627.
    • (1978) Science , vol.200 , pp. 618-627
    • Bell, G.I.1
  • 46
    • 0000755807 scopus 로고    scopus 로고
    • Affinity of trans-interacting VE-cadherin determined by atomic force microscopy
    • Baumgartner, W., H. J. Gruber, ..., D. Drenckhahn. 2000. Affinity of trans-interacting VE-cadherin determined by atomic force microscopy. Single Mol. 1:119-122.
    • (2000) Single Mol. , vol.1 , pp. 119-122
    • Baumgartner, W.1    Gruber, H.J.2    Drenckhahn, D.3
  • 47
    • 0000727648 scopus 로고
    • Studies in nonequilibrium rate processes. I. The relaxation of a system of harmonic oscillators
    • Montroll, E. W., and K. E. Shuler. 1957. Studies in nonequilibrium rate processes. I. The relaxation of a system of harmonic oscillators. J. Chem. Phys. 26:454-464.
    • (1957) J. Chem. Phys. , vol.26 , pp. 454-464
    • Montroll, E.W.1    Shuler, K.E.2
  • 49
    • 0038103565 scopus 로고    scopus 로고
    • X-ray snapshots of the maturation of an antibody response to a protein antigen
    • DOI 10.1038/nsb930
    • Li, Y., H. Li, ..., R. A. Mariuzza. 2003. X-ray snapshots of the maturation of an antibody response to a protein antigen. Nat. Struct. Biol. 10:482-488. (Pubitemid 36637647)
    • (2003) Nature Structural Biology , vol.10 , Issue.6 , pp. 482-488
    • Li, Y.1    Li, H.2    Yang, F.3    Smith-Gill, S.J.4    Mariuzza, R.A.5
  • 50
    • 0041009405 scopus 로고    scopus 로고
    • Association of the anti-hen egg lysozyme antibody HyHEL-5 with avian species variant and mutant lysozymes
    • Shick, K. A., K. A. Xavier, ..., R. C. Willson. 1997. Association of the anti-hen egg lysozyme antibody HyHEL-5 with avian species variant and mutant lysozymes. Biochim. Biophys. Acta. 1340:205-214.
    • (1997) Biochim. Biophys. Acta. , vol.1340 , pp. 205-214
    • Shick, K.A.1    Xavier, K.A.2    Willson, R.C.3
  • 54
    • 85031334317 scopus 로고    scopus 로고
    • Reference deleted in proof.
    • Reference deleted in proof.
  • 55
    • 0000495673 scopus 로고
    • Nucleation in supersaturated vapors. [Keimbildungsgeschwindigkeit in übersättigten. Dämpfen]
    • Farkas, L. 1927. Nucleation in supersaturated vapors. [Keimbildungsgeschwindigkeit in übersättigten. Dämpfen]. Z. Phys. Chem. 125: 236-242.
    • (1927) Z. Phys. Chem. , vol.125 , pp. 236-242
    • Farkas, L.1
  • 56
    • 0018410621 scopus 로고
    • Electric breakdown of bilayer lipid membranes. II. Calculation of the membrane lifetime in the steady-state diffusion approximation
    • DOI 10.1016/0302-4598(79)85006-0
    • Pastushenko, V. F., Y. A. Chizmadzhev, and V. B. Arakelyan. 1979. Electrical breakdown of bilayer lipid membranes. II. Calculation of the membrane lifetime in the steady-state diffusion approximation. Bioelectrochem. Bioenerg. 6:53-62. (Pubitemid 9199835)
    • (1979) Bioelectrochemistry and Bioenergetics , vol.6 , Issue.1 , pp. 53-62
    • Pastushenko, V.F.1    Chizmadzhev, Y.A.2    Arakelyan, V.B.3


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