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On the protein-protein diffusional encounter complex
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Brownian dynamics simulations were used to study the kinetics of barnase-barstar association. Four different models for the encounter complexes are compared and it is concluded that an encounter complex defined by a subset of native contacts provides the best agreement with experimental data.
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Gabdoulline R.R., Wade R.C. On the protein-protein diffusional encounter complex. J Mol Recognit. 12:1999;226-234. Brownian dynamics simulations were used to study the kinetics of barnase-barstar association. Four different models for the encounter complexes are compared and it is concluded that an encounter complex defined by a subset of native contacts provides the best agreement with experimental data.
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(1999)
J Mol Recognit
, vol.12
, pp. 226-234
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Gabdoulline, R.R.1
Wade, R.C.2
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52
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0029056922
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Energetics of protein-protein interactions: Analysis of the barnase-barstar interface by single mutations and double mutant cycles
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Schreiber G., Fersht A.R. Energetics of protein-protein interactions: analysis of the barnase-barstar interface by single mutations and double mutant cycles. J Mol Biol. 248:1995;478-486.
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(1995)
J Mol Biol
, vol.248
, pp. 478-486
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Schreiber, G.1
Fersht, A.R.2
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53
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0029873697
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Rapid, electrostatically assisted association of proteins
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Schreiber G., Fersht A.R. Rapid, electrostatically assisted association of proteins. Nat Struct Biol. 3:1996;427-431.
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(1996)
Nat Struct Biol
, vol.3
, pp. 427-431
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Schreiber, G.1
Fersht, A.R.2
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54
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0032557503
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Electrostatic enhancement of diffusion-controlled protein-protein asociation: Comparison of theory and experiment on barnase and barstar
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Calculations based on the transition-state theory and a particular structural model for the transition state are demonstrated to reproduce well the electrostatic enhancement of the association rate of a variety of mutants of the barnase-barstar complex.
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Vijayakumar M., Wong K.Y., Schreiber G., Fersht A.R., Szabo A., Zhou H-X. Electrostatic enhancement of diffusion-controlled protein-protein asociation: comparison of theory and experiment on barnase and barstar. J Mol Biol. 278:1998;1015-1024. Calculations based on the transition-state theory and a particular structural model for the transition state are demonstrated to reproduce well the electrostatic enhancement of the association rate of a variety of mutants of the barnase-barstar complex.
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(1998)
J Mol Biol
, vol.278
, pp. 1015-1024
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Vijayakumar, M.1
Wong, K.Y.2
Schreiber, G.3
Fersht, A.R.4
Szabo, A.5
Zhou, H.-X.6
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55
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0029998567
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Theory and simulation of the time-dependent rate coefficients of diffusion-influenced reactions
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Zhou H-X., Szabo A. Theory and simulation of the time-dependent rate coefficients of diffusion-influenced reactions. Biophys J. 71:1996;2440-2457.
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(1996)
Biophys J
, vol.71
, pp. 2440-2457
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Zhou, H.-X.1
Szabo, A.2
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56
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0033605858
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Predicting the rate enhancement of protein complex formation from the electrostatic energy of interaction
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Selzer T., Schreiber G. Predicting the rate enhancement of protein complex formation from the electrostatic energy of interaction. J Mol Biol. 287:1999;409-419.
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(1999)
J Mol Biol
, vol.287
, pp. 409-419
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Selzer, T.1
Schreiber, G.2
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57
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0344500752
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Computer simulation of protein-protein association kinetics: Acetylcholinesterase-fasciculin
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Brownian dynamics simulations were used to study the kinetics of acetylcholinesterase binding to its inhibitor fasciculin. Remarkably good agreement with a range of experimental data is reported. The nature of the encounter complex is discussed in light of the simulations.
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Elcock A.H., Gabdoulline R.R., Wade R.C., McCammon J.A. Computer simulation of protein-protein association kinetics: acetylcholinesterase-fasciculin. J Mol Biol. 291:1999;149-162. Brownian dynamics simulations were used to study the kinetics of acetylcholinesterase binding to its inhibitor fasciculin. Remarkably good agreement with a range of experimental data is reported. The nature of the encounter complex is discussed in light of the simulations.
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(1999)
J Mol Biol
, vol.291
, pp. 149-162
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Elcock, A.H.1
Gabdoulline, R.R.2
Wade, R.C.3
McCammon, J.A.4
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58
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0032981961
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Free energy landscapes of encounter complexes in protein-protein association
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The energies of diffusion-accessible encounter conformations are examined for four protein-protein complexes. Partial desolvation effects are found to be significant for the stabilization of the conformations surrounding the binding site and, thus, promote association.
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Camacho C.J., Weng Z., Vajda S., DeLisi C. Free energy landscapes of encounter complexes in protein-protein association. Biophys J. 76:1999;1166-1178. The energies of diffusion-accessible encounter conformations are examined for four protein-protein complexes. Partial desolvation effects are found to be significant for the stabilization of the conformations surrounding the binding site and, thus, promote association.
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(1999)
Biophys J
, vol.76
, pp. 1166-1178
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Camacho, C.J.1
Weng, Z.2
Vajda, S.3
DeLisi, C.4
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