메뉴 건너뛰기




Volumn 73, Issue 5, 1997, Pages 2441-2445

Enhancement of protein-protein association rate by interaction potential: Accuracy of prediction based on local Boltzmann factor

Author keywords

[No Author keywords available]

Indexed keywords

ACCURACY; ARTICLE; DIFFUSION; ELECTRIC POTENTIAL; PREDICTION; PROTEIN PROTEIN INTERACTION;

EID: 0030734751     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(97)78272-9     Document Type: Article
Times cited : (55)

References (27)
  • 2
    • 0022087686 scopus 로고
    • Simulation of the diffusion-controlled reaction between superoxide and superoxide dismutase. I. Simple models
    • Allison, S. A., G. Ganti, and J. A. McCammon. 1985. Simulation of the diffusion-controlled reaction between superoxide and superoxide dismutase. I. Simple models. Biopolymers. 24:1323-1336.
    • (1985) Biopolymers , vol.24 , pp. 1323-1336
    • Allison, S.A.1    Ganti, G.2    McCammon, J.A.3
  • 3
    • 0343870188 scopus 로고
    • Model potentials in kinetics of interacting particles
    • Belyi, A. A. 1984. Model potentials in kinetics of interacting particles. Zh. Fiz. Khim. 58:2189-2193.
    • (1984) Zh. Fiz. Khim. , vol.58 , pp. 2189-2193
    • Belyi, A.A.1
  • 4
    • 0021904674 scopus 로고
    • Orientation constraints in diffusion-limited macromolecular association. the role of surface diffusion as a rate-enhancing mechanism
    • Berg, O. G. 1985. Orientation constraints in diffusion-limited macromolecular association. The role of surface diffusion as a rate-enhancing mechanism. Biophys. J. 47:1-14.
    • (1985) Biophys. J. , vol.47 , pp. 1-14
    • Berg, O.G.1
  • 5
    • 0041973544 scopus 로고
    • Diffusion-controlled reactions on an active site
    • Doktorov, A. B., and N. N. Lukzen. 1981. Diffusion-controlled reactions on an active site. Chem. Phys. Lett. 79:498-502.
    • (1981) Chem. Phys. Lett. , vol.79 , pp. 498-502
    • Doktorov, A.B.1    Lukzen, N.N.2
  • 7
    • 33748501925 scopus 로고    scopus 로고
    • Effective charges for macromolecules in solvent
    • Gabdoulline, R. R., and R. C. Wade. 1996. Effective charges for macromolecules in solvent. J. Phys. Chem. 100:3868-3878.
    • (1996) J. Phys. Chem. , vol.100 , pp. 3868-3878
    • Gabdoulline, R.R.1    Wade, R.C.2
  • 8
    • 0030891436 scopus 로고    scopus 로고
    • Simulation of the diffusional association of barnase and barstar
    • Gabdoulline, R. R., and R. C. Wade. 1997. Simulation of the diffusional association of barnase and barstar. Biophys. J. 72:1917-1929.
    • (1997) Biophys. J. , vol.72 , pp. 1917-1929
    • Gabdoulline, R.R.1    Wade, R.C.2
  • 9
    • 0028919738 scopus 로고
    • Computer modeling of electrostatic steering and orientational effects in antibody- antigen association
    • Kozack, R. R., M. J. d'Mello, and S. Subramaniam. 1995. Computer modeling of electrostatic steering and orientational effects in antibody- antigen association. Biophys. J. 68:807-814.
    • (1995) Biophys. J. , vol.68 , pp. 807-814
    • Kozack, R.R.1    D'Mello, M.J.2    Subramaniam, S.3
  • 10
    • 0001315530 scopus 로고
    • Intermolecular interaction between bovine pancreatic trypsin inhibitor molecules probed by Brownian dynamics simulation
    • Nambi, P., A. Wierzbicki, and S. A. Allison. 1991. Intermolecular interaction between bovine pancreatic trypsin inhibitor molecules probed by Brownian dynamics simulation. J. Phys. Chem. 95:9595-9600.
    • (1991) J. Phys. Chem. , vol.95 , pp. 9595-9600
    • Nambi, P.1    Wierzbicki, A.2    Allison, S.A.3
  • 11
    • 36549102274 scopus 로고
    • Brownian dynamics simulation of diffusion-influenced bimolecular reactions
    • Northrup, S. H., S. A. Allison, and J. A. McCammon. 1984. Brownian dynamics simulation of diffusion-influenced bimolecular reactions. J. Chem. Phys. 80:1517-1524.
    • (1984) J. Chem. Phys. , vol.80 , pp. 1517-1524
    • Northrup, S.H.1    Allison, S.A.2    McCammon, J.A.3
  • 12
    • 33845282908 scopus 로고
    • Electrostatic effects in the Brownian dynamics of association and orientation of heme proteins
    • Nonthrup, S. H., J. O. Boles, and J. C. L. Reynolds. 1987. Electrostatic effects in the Brownian dynamics of association and orientation of heme proteins. J. Phys. Chem. 91:5991-5998.
    • (1987) J. Phys. Chem. , vol.91 , pp. 5991-5998
    • Nonthrup, S.H.1    Boles, J.O.2    Reynolds, J.C.L.3
  • 15
    • 0027177102 scopus 로고
    • The interaction of barnase with its polypeptide inhibitor barstar studied by protein engineering
    • Schreiber, G., and A. R. Fersht. 1993. The interaction of barnase with its polypeptide inhibitor barstar studied by protein engineering. Biochemistry. 32:5145-5150.
    • (1993) Biochemistry , vol.32 , pp. 5145-5150
    • Schreiber, G.1    Fersht, A.R.2
  • 16
    • 0029873697 scopus 로고    scopus 로고
    • Rapid, electrostatically assisted association of proteins
    • Schreiber, G., and A. R. Fersht. 1996. Rapid, electrostatically assisted association of proteins. Nature Struct. Biol. 3:427-431.
    • (1996) Nature Struct. Biol. , vol.3 , pp. 427-431
    • Schreiber, G.1    Fersht, A.R.2
  • 17
    • 0019763827 scopus 로고
    • Diffusion-controlled bimolecular reaction rates. the effect of rotational diffusion and orientation constraints
    • Shoup, D., G. Lipari, and A. Szabo. 1981. Diffusion-controlled bimolecular reaction rates. The effect of rotational diffusion and orientation constraints, Biophys. J. 36:697-714.
    • (1981) Biophys. J. , vol.36 , pp. 697-714
    • Shoup, D.1    Lipari, G.2    Szabo, A.3
  • 18
    • 0000267310 scopus 로고
    • Versuch einer mathematischen theorie der koagulationskinetik kolloider losungen
    • Smoluchowski, M. V. 1917. Versuch einer mathematischen theorie der koagulationskinetik kolloider losungen. Z. Phys. Chem. 92:129-168.
    • (1917) Z. Phys. Chem. , vol.92 , pp. 129-168
    • Smoluchowski, M.V.1
  • 19
    • 0024466381 scopus 로고
    • Quantitative evaluation of the contribution of ionic interactions to the formation of the thrombin-hirudin complex
    • Stones, R. S., S. Dennis, and J. Hofsteenge. 1989. Quantitative evaluation of the contribution of ionic interactions to the formation of the thrombin-hirudin complex. Biochemistry. 28:6857-6863.
    • (1989) Biochemistry , vol.28 , pp. 6857-6863
    • Stones, R.S.1    Dennis, S.2    Hofsteenge, J.3
  • 20
    • 0008012064 scopus 로고
    • Diffusion-controlled reaction rate to asymmetric reactants under Coulomb interaction
    • Traytak, S. D., and M. Tachiya. 1995. Diffusion-controlled reaction rate to asymmetric reactants under Coulomb interaction. J. Chem. Phys. 102: 9240-9247.
    • (1995) J. Chem. Phys. , vol.102 , pp. 9240-9247
    • Traytak, S.D.1    Tachiya, M.2
  • 21
    • 0028866770 scopus 로고
    • Protein- Protein interactions in colicin E9 DNase-immunity protein complexes. 1. Diffusion-controlled association and femtomolar binding for the cognate complex
    • Wallis, R., G. R. Moore, R. James, and C. Kleanthous. 1995. Protein- protein interactions in colicin E9 DNase-immunity protein complexes. 1. Diffusion-controlled association and femtomolar binding for the cognate complex. Biochemistry. 34:13743-13750.
    • (1995) Biochemistry , vol.34 , pp. 13743-13750
    • Wallis, R.1    Moore, G.R.2    James, R.3    Kleanthous, C.4
  • 22
    • 0031012271 scopus 로고    scopus 로고
    • Very rapid, ionic strength-dependent association and folding of a heterodimeric leucine zipper
    • Wendt, H., L. Leder, H. Harma, I. Jelesarov, A. Baici, and H. R. Bosshard. 1997. Very rapid, ionic strength-dependent association and folding of a heterodimeric leucine zipper. Biochemistry. 36:204-213.
    • (1997) Biochemistry , vol.36 , pp. 204-213
    • Wendt, H.1    Leder, L.2    Harma, H.3    Jelesarov, I.4    Baici, A.5    Bosshard, H.R.6
  • 23
    • 0027161336 scopus 로고
    • Brownian dynamics study of the influences of electrostatic interaction and diffusion on protein-protein association kinetics
    • Zhou, H.-X. 1993a. Brownian dynamics study of the influences of electrostatic interaction and diffusion on protein-protein association kinetics. Biophys. J. 64:1711-1726.
    • (1993) Biophys. J. , vol.64 , pp. 1711-1726
    • Zhou, H.-X.1
  • 24
    • 0027254625 scopus 로고
    • Boundary element solution of macromolecular electrostatics: Interaction energy between two proteins
    • Zhou, H.-X. 1993b. Boundary element solution of macromolecular electrostatics: interaction energy between two proteins. Biophys. J. 65: 955-963.
    • (1993) Biophys. J. , vol.65 , pp. 955-963
    • Zhou, H.-X.1
  • 25
    • 0000827703 scopus 로고    scopus 로고
    • Effect of interaction potentials in diffusion-influenced reactions with small reactive regions
    • Thou, H.-X. 1996, Effect of interaction potentials in diffusion-influenced reactions with small reactive regions. J. Chem. Phys. 105:7235-7237.
    • (1996) J. Chem. Phys. , vol.105 , pp. 7235-7237
    • Thou, H.-X.1
  • 26
    • 0030462735 scopus 로고    scopus 로고
    • A 240-fold electrostatic rate-enhancement for acetylcholinesterase-substrate binding can be predicted by the potential within the active site
    • Zhou, H.-X., J. M. Briggs, and J. A. McCammon. 1996. A 240-fold electrostatic rate-enhancement for acetylcholinesterase-substrate binding can be predicted by the potential within the active site. J. Am. Chem. Soc. 118:13069-13070.
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 13069-13070
    • Zhou, H.-X.1    Briggs, J.M.2    McCammon, J.A.3
  • 27
    • 0029998567 scopus 로고    scopus 로고
    • Theory and simulation of the time- Dependent rate coefficients of diffusion-influenced reactions
    • Zhou, H.-X., and A. Szabo. 1996. Theory and simulation of the time- dependent rate coefficients of diffusion-influenced reactions. Biophys. J. 71:2440-2457.
    • (1996) Biophys. J. , vol.71 , pp. 2440-2457
    • Zhou, H.-X.1    Szabo, A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.