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Volumn 52, Issue 3, 2006, Pages 277-289

An asymptotic comparative analysis of the thermodynamics of non-covalent association

Author keywords

Brownian dynamics; Laplace's method of integration; Macromolecular mechanics; Nano biochemistry; Transition state

Indexed keywords

ION; LIGAND; PROTEIN;

EID: 32544457557     PISSN: 03036812     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00285-005-0353-3     Document Type: Article
Times cited : (9)

References (41)
  • 1
    • 0030917908 scopus 로고    scopus 로고
    • Loss of translational entropy in binding, folding, and catalysis
    • Amzel, L.M.: Loss of translational entropy in binding, folding, and catalysis. Prot: Struct. Funct. Genet. 28, 144-149 (1997)
    • (1997) Prot: Struct. Funct. Genet. , vol.28 , pp. 144-149
    • Amzel, L.M.1
  • 2
    • 0030872242 scopus 로고    scopus 로고
    • Reconstructing potential energy functions from simulated force-induced unbinding processes
    • Balsera, M., Stepaniants, S., Izrailev, S., Oono, Y., Schulten, K.: Reconstructing potential energy functions from simulated force-induced unbinding processes. Biophys. J. 73, 1281-1287 (1997)
    • (1997) Biophys. J. , vol.73 , pp. 1281-1287
    • Balsera, M.1    Stepaniants, S.2    Izrailev, S.3    Oono, Y.4    Schulten, K.5
  • 4
    • 3943103200 scopus 로고
    • Standard thermodynamics of transfer. Uses and misuses
    • Ben-Naim, A.: Standard thermodynamics of transfer. Uses and misuses. J. Phys. Chem. 82, 792-803, (1978)
    • (1978) J. Phys. Chem. , vol.82 , pp. 792-803
    • Ben-Naim, A.1
  • 6
    • 0028853559 scopus 로고
    • The relationship between ligand-binding thermodynamics and protein-ligand interaction forces measured by atomic force microscopy
    • Chilkoti, A., Boland, T., Ratner, B.D., Stayton, P.S.: The relationship between ligand-binding thermodynamics and protein-ligand interaction forces measured by atomic force microscopy.Biophys. J. 69, 2125-2130 (1995)
    • (1995) Biophys. J. , vol.69 , pp. 2125-2130
    • Chilkoti, A.1    Boland, T.2    Ratner, B.D.3    Stayton, P.S.4
  • 7
    • 0028910003 scopus 로고
    • Site-directed mutagenesis studies of the high-affinity streptavidin-biotin complex: Contributions of tryptophan residues 79, 108, and 120
    • USA
    • Chilkoti, A., Tan, P.H., Stayton, P.S.: Site-directed mutagenesis studies of the high-affinity streptavidin-biotin complex: contributions of tryptophan residues 79, 108, and 120. Proc. Natl. Acad. Sci. USA 92, 1754-1758 (1995)
    • (1995) Proc. Natl. Acad. Sci. , vol.92 , pp. 1754-1758
    • Chilkoti, A.1    Tan, P.H.2    Stayton, P.S.3
  • 8
    • 0000134186 scopus 로고
    • Theory of the stability of strongly charged lyophobic sols and of the adhesion of strongly charged particles in solutions of electrolytes
    • Derjaguin, B., Landau, L.: Theory of the stability of strongly charged lyophobic sols and of the adhesion of strongly charged particles in solutions of electrolytes. Acta Physicochim. U.R.S.S. 14, 633-662 (1941)
    • (1941) Acta Physicochim. U.R.S.S. , vol.14 , pp. 633-662
    • Derjaguin, B.1    Landau, L.2
  • 9
    • 0030733858 scopus 로고    scopus 로고
    • Local interactions and the optimization of protein folding
    • Doyle, R., Simons, K., Qian, H., Baker, D.: Local interactions and the optimization of protein folding. Prot: Struct. Funct. Genet. 29, 282-291 (1997)
    • (1997) Prot: Struct. Funct. Genet. , vol.29 , pp. 282-291
    • Doyle, R.1    Simons, K.2    Qian, H.3    Baker, D.4
  • 10
    • 0031001349 scopus 로고    scopus 로고
    • Dynamic strength of molecular adhesion bonds
    • Evans, E., Ritchie, K.: Dynamic strength of molecular adhesion bonds. Biophys. J. 72, 1541-1555 (1997)
    • (1997) Biophys. J. , vol.72 , pp. 1541-1555
    • Evans, E.1    Ritchie, K.2
  • 11
    • 0028309424 scopus 로고
    • Adhesion forces between individual ligand-receptor pairs
    • Florin, E., Moy, V.T., Gaub, H.E.: Adhesion forces between individual ligand-receptor pairs. Science 264, 415-417 (1994)
    • (1994) Science , vol.264 , pp. 415-417
    • Florin, E.1    Moy, V.T.2    Gaub, H.E.3
  • 12
    • 0031058541 scopus 로고    scopus 로고
    • The statistical-thermodynamic basis for computation of binding affinities: A critical review
    • Gilson, M.K., Given, J.A., Bush, B.L., McCammon, J.A.: The statistical-thermodynamic basis for computation of binding affinities: a critical review. Biophys. J. 72, 1047-1069 (1997)
    • (1997) Biophys. J. , vol.72 , pp. 1047-1069
    • Gilson, M.K.1    Given, J.A.2    Bush, B.L.3    McCammon, J.A.4
  • 13
    • 0030059225 scopus 로고    scopus 로고
    • Ligand binding: Molecular mechanics calculation of the streptavidin-biotin rupture force
    • Grubmüller, H., Heymann, B., Tavan, P.: Ligand binding: molecular mechanics calculation of the streptavidin-biotin rupture force. Science 271, 997-999 (1996)
    • (1996) Science , vol.271 , pp. 997-999
    • Grubmüller, H.1    Heymann, B.2    Tavan, P.3
  • 14
    • 36849129750 scopus 로고
    • Theory of protein solutions
    • Hill, T.L.: Theory of protein solutions. I.J. Chem. Phys. 23, 623-636 (1955)
    • (1955) I.J. Chem. Phys. , vol.23 , pp. 623-636
    • Hill, T.L.1
  • 16
    • 0000846782 scopus 로고
    • Effect of rotation on the diffusion-controlled rate of ligand-protein association
    • USA
    • Hill, T.L.: Effect of rotation on the diffusion-controlled rate of ligand-protein association.Proc. Natl. Acad. Sci. USA 72, 4918-4922 (1975)
    • (1975) Proc. Natl. Acad. Sci. , vol.72 , pp. 4918-4922
    • Hill, T.L.1
  • 17
    • 0016927165 scopus 로고
    • Diffusion frequency factors in some simple examples of transition-state rate theory
    • USA
    • Hill, T.L.: Diffusion frequency factors in some simple examples of transition-state rate theory. Proc. Natl. Acad. Sci. USA 73, 679-683 (1976)
    • (1976) Proc. Natl. Acad. Sci. , vol.73 , pp. 679-683
    • Hill, T.L.1
  • 18
    • 0030987036 scopus 로고    scopus 로고
    • Molecular dynamics study of unbinding of the avidin-biotin complex
    • Izrailev, S., Stepaniants, S., Balsera, M., Oono, Y., Schulten, K.: Molecular dynamics study of unbinding of the avidin-biotin complex. Biophys. J. 72, 1568-1581 (1997)
    • (1997) Biophys. J. , vol.72 , pp. 1568-1581
    • Izrailev, S.1    Stepaniants, S.2    Balsera, M.3    Oono, Y.4    Schulten, K.5
  • 20
    • 33751132430 scopus 로고
    • The statistical mechanical theory of solution
    • Kirkwood, J., Buff, F.: The statistical mechanical theory of solution. I.J. Chem. Phys. 19, 774-777 (1951)
    • (1951) I.J. Chem. Phys. , vol.19 , pp. 774-777
    • Kirkwood, J.1    Buff, F.2
  • 21
    • 34547275473 scopus 로고
    • Brownian motion in a field of force and the diffusion model of chemical reactions
    • Kramers, H.A.: Brownian motion in a field of force and the diffusion model of chemical reactions. Physica 7, 284-304 (1940)
    • (1940) Physica , vol.7 , pp. 284-304
    • Kramers, H.A.1
  • 22
    • 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.: Energy landscapes of receptor-ligand bonds explored with dynamic force spectroscopy. Nature 397, 50-53 (1999)
    • (1999) Nature , vol.397 , pp. 50-53
    • Merkel, R.1    Nassoy, P.2    Leung, A.3    Ritchie, K.4    Evans, E.5
  • 23
    • 0028140707 scopus 로고
    • Intermolecular forces and energies between ligands and receptors
    • Moy, V.T., Florin, E., Gaub, H.E.: Intermolecular forces and energies between ligands and receptors. Science 266, 257-259 (1994)
    • (1994) Science , vol.266 , pp. 257-259
    • Moy, V.T.1    Florin, E.2    Gaub, H.E.3
  • 25
    • 0001199087 scopus 로고    scopus 로고
    • Entropy-enthalpy compensation: Conformational fluctuation and induced-fit
    • Qian, H.: Entropy-enthalpy compensation: conformational fluctuation and induced-fit. J. Chem. Phys. 109, 10015-10017 (1998)
    • (1998) J. Chem. Phys. , vol.109 , pp. 10015-10017
    • Qian, H.1
  • 26
    • 0034303054 scopus 로고    scopus 로고
    • A mathematical analysis of the Brownian dynamics of DNA tether
    • Qian, H.: A mathematical analysis of the Brownian dynamics of DNA tether. J. Math. Biol. 41, 331-340 (2000)
    • (2000) J. Math. Biol. , vol.41 , pp. 331-340
    • Qian, H.1
  • 28
    • 0036135425 scopus 로고    scopus 로고
    • From discrete protein kinetics to continuous Brownian dynamics: A new perspective
    • Qian, H.: From discrete protein kinetics to continuous Brownian dynamics: a new perspective. Prot. Sci. 11, 1-5 (2002)
    • (2002) Prot. Sci. , vol.11 , pp. 1-5
    • Qian, H.1
  • 29
    • 33645831413 scopus 로고    scopus 로고
    • Entropy-enthalpy compensation: Perturbation and relaxation in thermodynamic systems
    • Qian, H., Hopfield, J.J.: Entropy-enthalpy compensation: perturbation and relaxation in thermodynamic systems. J. Chem. Phys. 105, 9292-9296 (1996)
    • (1996) J. Chem. Phys. , vol.105 , pp. 9292-9296
    • Qian, H.1    Hopfield, J.J.2
  • 30
    • 0032756253 scopus 로고    scopus 로고
    • A graphical method for force analysis: Macromolecular mechanics with atomic force microscopy
    • Qian, H., Shapiro, B.E.: A graphical method for force analysis: macromolecular mechanics with atomic force microscopy. Prot: Struct. Funct. Genet. 37, 576-581 (1999)
    • (1999) Prot: Struct. Funct. Genet. , vol.37 , pp. 576-581
    • Qian, H.1    Shapiro, B.E.2
  • 31
    • 0034505344 scopus 로고    scopus 로고
    • Transformed Poisson-Boltzmann relations and ionic distributions
    • Qian, H., Schellman, J.A.: Transformed Poisson-Boltzmann relations and ionic distributions. J. Phys. Chem. B 104, 11528-11540 (2000)
    • (2000) J. Phys. Chem. B , vol.104 , pp. 11528-11540
    • Qian, H.1    Schellman, J.A.2
  • 32
    • 0002278843 scopus 로고
    • Scaled particle methods in the statistical thermodynamics of fluids
    • Reiss, H.: Scaled particle methods in the statistical thermodynamics of fluids. Adv. Chem. Phys. 9, 1-84 (1965)
    • (1965) Adv. Chem. Phys. , vol.9 , pp. 1-84
    • Reiss, H.1
  • 33
    • 0017802519 scopus 로고
    • Solvent denaturation
    • Schellman, J.A.: Solvent denaturation. Biopolymers 17, 1305-1322 (1978)
    • (1978) Biopolymers , vol.17 , pp. 1305-1322
    • Schellman, J.A.1
  • 34
    • 0025174790 scopus 로고
    • Fluctuation and linkage relations in macromolecular solution
    • Schellman, J.A.: Fluctuation and linkage relations in macromolecular solution. Biopolymers 29, 215-224 (1990)
    • (1990) Biopolymers , vol.29 , pp. 215-224
    • Schellman, J.A.1
  • 35
    • 0027470443 scopus 로고
    • The relation between the free energy of ineraction and binding
    • Schellman, J.A.: The relation between the free energy of ineraction and binding. Biophys. Chem. 45, 273-279 (1993)
    • (1993) Biophys. Chem. , vol.45 , pp. 273-279
    • Schellman, J.A.1
  • 37
    • 0030729125 scopus 로고    scopus 로고
    • A quantitative analysis of single protein-ligand complex separation with the atomic force microscope
    • Shapiro, B.E., Qian, H.: A quantitative analysis of single protein-ligand complex separation with the atomic force microscope. Biophys. Chem. 67, 211-219 (1997)
    • (1997) Biophys. Chem. , vol.67 , pp. 211-219
    • Shapiro, B.E.1    Qian, H.2
  • 38
    • 0032556183 scopus 로고    scopus 로고
    • Hysteresis in force probe measurements: A dynamic systems perspective
    • Shapiro, B.E., Qian, H.: Hysteresis in force probe measurements: a dynamic systems perspective. J. Theoret. Biol. 194, 551-559 (1998)
    • (1998) J. Theoret. Biol. , vol.194 , pp. 551-559
    • Shapiro, B.E.1    Qian, H.2
  • 39
    • 36749116443 scopus 로고
    • First passage time approach to diffusion controlled reactions
    • Szabo, A., Schulten, K., Schulten, Z.: First passage time approach to diffusion controlled reactions. J. Chem. Phys. 72, 4350-4357 (1980)
    • (1980) J. Chem. Phys. , vol.72 , pp. 4350-4357
    • Szabo, A.1    Schulten, K.2    Schulten, Z.3
  • 40
    • 0031016904 scopus 로고    scopus 로고
    • Direct measurement of a tethered ligand-receptor interaction potential
    • Wong, J.Y., Kuhl, T.L., Israelachvili, J.N., Mullah, N., Zalipsky, S.: Direct measurement of a tethered ligand-receptor interaction potential. Science 275, 820-822 (1997)
    • (1997) Science , vol.275 , pp. 820-822
    • Wong, J.Y.1    Kuhl, T.L.2    Israelachvili, J.N.3    Mullah, N.4    Zalipsky, S.5
  • 41
    • 0028882223 scopus 로고
    • Simple model of protein folding kinetics
    • USA
    • Zwanzig, R.: Simple model of protein folding kinetics. Proc. Natl. Acad. Sci. USA 92, 9801-9804 (1995)
    • (1995) Proc. Natl. Acad. Sci. , vol.92 , pp. 9801-9804
    • Zwanzig, R.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.