메뉴 건너뛰기




Volumn 287, Issue 2, 1999, Pages 409-419

Predicting the rate enhancement of protein complex formation from the electrostatic energy of interaction

Author keywords

Electrostatic rate enhancement; Protein association; Protein complexes; Protein engineering

Indexed keywords

ACETYLCHOLINESTERASE; BARNASE; FASCICULIN; HIRUDIN; THROMBIN;

EID: 0033605858     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1999.2615     Document Type: Article
Times cited : (116)

References (31)
  • 1
    • 0023651197 scopus 로고
    • Abnormal solubility behavior of beta-lactoglobulin: Salting-in by glycine and NaCl
    • Arakawa T., Timasheff S. N. Abnormal solubility behavior of beta-lactoglobulin: salting-in by glycine and NaCl. Biochemistry. 1987;265147-265153.
    • (1987) Biochemistry , pp. 265147-265153
    • Arakawa, T.1    Timasheff, S.N.2
  • 3
    • 0028818897 scopus 로고
    • Acetylcholinesterase inhibition by fasciculin: Crystal structue of the complex
    • Bourne Y., Taylor P., Marchot P. Acetylcholinesterase inhibition by fasciculin: crystal structue of the complex. Cell. 83:1995;503-512.
    • (1995) Cell , vol.83 , pp. 503-512
    • Bourne, Y.1    Taylor, P.2    Marchot, P.3
  • 4
    • 0028074974 scopus 로고
    • Protein-protein recognition: Crystal structural analysis of a barnase-barstar complex at 2.0-Å resolution
    • Buckle M., Schreiber G., Fersht A. R. Protein-protein recognition: crystal structural analysis of a barnase-barstar complex at 2.0-Å resolution. Biochemistry. 33:1994;8878-8889.
    • (1994) Biochemistry , vol.33 , pp. 8878-8889
    • Buckle, M.1    Schreiber, G.2    Fersht, A.R.3
  • 5
    • 0030727624 scopus 로고    scopus 로고
    • The Hofmeister series: Salt and solvent effects on interfacial phenomena
    • Cacace M. G., Landau E. M., Ramsden J. J. The Hofmeister series: salt and solvent effects on interfacial phenomena. Quart. Rev. Biophys. 30:1997;241-277.
    • (1997) Quart. Rev. Biophys. , vol.30 , pp. 241-277
    • Cacace, M.G.1    Landau, E.M.2    Ramsden, J.J.3
  • 6
    • 0039789834 scopus 로고
    • Elementary steps in enzyme reactions
    • Eigen M., Hammes G. G. Elementary steps in enzyme reactions. Advan. Enzymol. 25:1963;1-38.
    • (1963) Advan. Enzymol. , vol.25 , pp. 1-38
    • Eigen, M.1    Hammes, G.G.2
  • 7
    • 0023662562 scopus 로고
    • Structure-activity relationships in engineered proteins: Analysis of use of binding energy by linear free energy relationships
    • Fersht A. R., Leatherbarrow R. J., Wells T. N. C. Structure-activity relationships in engineered proteins: analysis of use of binding energy by linear free energy relationships. Biochemistry. 26:1987;6030-6038.
    • (1987) Biochemistry , vol.26 , pp. 6030-6038
    • Fersht, A.R.1    Leatherbarrow, R.J.2    Wells, T.N.C.3
  • 8
    • 0026511656 scopus 로고
    • The folding of an enzyme I: Theory of protein engineering analysis of stability and pathway of protein folding
    • Fersht A. R., Matouschek A., Serrano L. The folding of an enzyme I: Theory of protein engineering analysis of stability and pathway of protein folding. J. Mol. Biol. 224:1992;771-782.
    • (1992) J. Mol. Biol. , vol.224 , pp. 771-782
    • Fersht, A.R.1    Matouschek, A.2    Serrano, L.3
  • 9
    • 0030891436 scopus 로고    scopus 로고
    • Simulation of the diffusional association of barnase and barstar
    • Gabdoulline R. R., Wade R. C. Simulation of the diffusional association of barnase and barstar. Biophys. J. 72:1997;1917-1929.
    • (1997) Biophys. J. , vol.72 , pp. 1917-1929
    • Gabdoulline, R.R.1    Wade, R.C.2
  • 10
    • 0031473847 scopus 로고    scopus 로고
    • SWISS-MODEL and the Swiss-PdbViewer: An environment for comparative protein modeling
    • Guex N., Peitsch M. C. SWISS-MODEL and the Swiss-PdbViewer: An environment for comparative protein modeling. Electrophoresis. 18:1997;2714-2723.
    • (1997) Electrophoresis. , vol.18 , pp. 2714-2723
    • Guex, N.1    Peitsch, M.C.2
  • 11
    • 0029646114 scopus 로고
    • Crystal structure of an acetylcholinesterase-fasciculin complex: Interaction of a three-fingered toxin from snake venom with its target
    • Harel M., Kleywegt G. J., Ravelli R. B., Silman I., Sussman J. L. Crystal structure of an acetylcholinesterase-fasciculin complex: interaction of a three-fingered toxin from snake venom with its target. Structure. 3:1995;1355-1366.
    • (1995) Structure , vol.3 , pp. 1355-1366
    • Harel, M.1    Kleywegt, G.J.2    Ravelli, R.B.3    Silman, I.4    Sussman, J.L.5
  • 12
    • 0028919738 scopus 로고
    • Computer modeling of electrostatic steering and orientational effects in antibody-antigen association
    • Kozack U. E., d'Mello M. J., Subramanian S. Computer modeling of electrostatic steering and orientational effects in antibody-antigen association. Biophys. J. 68:1995;807-814.
    • (1995) Biophys. J. , vol.68 , pp. 807-814
    • Kozack, U.E.1    D'Mello, M.J.2    Subramanian, S.3
  • 13
    • 0026613082 scopus 로고
    • 1.9 Angstrom resolution structure of fasciculin 1, an anti-acetylcholinesterase toxin from green Mamba
    • Le-Du M. H., Marchot P., Bougis P. E., Fontecilla-Camps J. C. 1.9 Angstrom resolution structure of fasciculin 1, an anti-acetylcholinesterase toxin from green Mamba. J. Biol. Chem. 267:1992;22122.
    • (1992) J. Biol. Chem. , vol.267 , pp. 22122
    • Le-Du, M.H.1    Marchot, P.2    Bougis, P.E.3    Fontecilla-Camps, J.C.4
  • 14
    • 84962439356 scopus 로고    scopus 로고
    • Roles of electrostatic interaction in proteins
    • Nakamura H. Roles of electrostatic interaction in proteins. Quart. Rev. Biophys. 29:1996;1-90.
    • (1996) Quart. Rev. Biophys. , vol.29 , pp. 1-90
    • Nakamura, H.1
  • 16
    • 0030828982 scopus 로고    scopus 로고
    • Electrostatic influence of the kinetic of ligand binding to acetylcholinesterase
    • Radic Z., Kirchhoff P. D., Quinn D. M., McCammon A., Taylor P. Electrostatic influence of the kinetic of ligand binding to acetylcholinesterase. J. Biol. Chem. 37:1997;23265-23277.
    • (1997) J. Biol. Chem. , vol.37 , pp. 23265-23277
    • Radic, Z.1    Kirchhoff, P.D.2    Quinn, D.M.3    McCammon, A.4    Taylor, P.5
  • 18
    • 0027177102 scopus 로고
    • The Interaction of barnase with its polypeptide inhibitor barstar studied by protein engineering
    • Schreiber G., Fersht A. R. The Interaction of barnase with its polypeptide inhibitor barstar studied by protein engineering. Biochemistry. 32:1993;5145-5150.
    • (1993) Biochemistry , vol.32 , pp. 5145-5150
    • Schreiber, G.1    Fersht, A.R.2
  • 19
    • 0029873697 scopus 로고    scopus 로고
    • Rapid, electrostatic assisted, association of proteins
    • Schreiber G., Fersht A. R. Rapid, electrostatic assisted, association of proteins. Nature Struct. Biol. 3:1996;427-431.
    • (1996) Nature Struct. Biol. , vol.3 , pp. 427-431
    • Schreiber, G.1    Fersht, A.R.2
  • 20
    • 0028774340 scopus 로고
    • Stability versus function: Two competing forces in the evolution of barstar
    • Schreiber G., Buckle A. M., Fersht A. R. Stability versus function: two competing forces in the evolution of barstar. Structure. 2:1994;945-951.
    • (1994) Structure , vol.2 , pp. 945-951
    • Schreiber, G.1    Buckle, A.M.2    Fersht, A.R.3
  • 21
    • 0010624785 scopus 로고    scopus 로고
    • The effect of protein relaxation on charge-charge interactions and dielectric constants of proteins
    • Sham Y. Y., Muegge I., Warshel A. The effect of protein relaxation on charge-charge interactions and dielectric constants of proteins. Biophys. J. 74:1998;1744-1753.
    • (1998) Biophys. J. , vol.74 , pp. 1744-1753
    • Sham, Y.Y.1    Muegge, I.2    Warshel, A.3
  • 22
    • 32844457567 scopus 로고
    • Accurate calculation of hydration free energies using macroscopic solvent models
    • Sitkoff D., Sharp K. A., Honig B. Accurate calculation of hydration free energies using macroscopic solvent models. J. Phys. Chem. 98:1994;1978-1988.
    • (1994) J. Phys. Chem. , vol.98 , pp. 1978-1988
    • Sitkoff, D.1    Sharp, K.A.2    Honig, B.3
  • 23
    • 0024466381 scopus 로고
    • Quantitative evaluation of the contribution of ionic interactions to the formation of the thrombin-hirudin complex
    • Stone R. S., Dennis S., Hofsteenge J. Quantitative evaluation of the contribution of ionic interactions to the formation of the thrombin-hirudin complex. Biochemistry. 28:1989;6857-6863.
    • (1989) Biochemistry , vol.28 , pp. 6857-6863
    • Stone, R.S.1    Dennis, S.2    Hofsteenge, J.3
  • 24
    • 0032491205 scopus 로고    scopus 로고
    • Transient kinetic studies on the interaction of Ras and the Ras-binding domain of c-Raf-1 reveal rapid equilibration of the complex
    • Sydor J. R., Engelhard M., Wittinghofer A., Goody R. S., Herrmann C. Transient kinetic studies on the interaction of Ras and the Ras-binding domain of c-Raf-1 reveal rapid equilibration of the complex. Biochemistry. 37:1998;14292-14299.
    • (1998) Biochemistry , vol.37 , pp. 14292-14299
    • Sydor, J.R.1    Engelhard, M.2    Wittinghofer, A.3    Goody, R.S.4    Herrmann, C.5
  • 25
    • 0027055006 scopus 로고
    • Impact of protein-protein contacts on the conformation of thrombin-bound hirudin studied by comparison with the nuclear magnetic resonance solution structure of hirudin(1-51)
    • Szyperski T., Guntert P., Stone S. R., Tulinsky A., Bode W., Huber R., Wuthrich K. Impact of protein-protein contacts on the conformation of thrombin-bound hirudin studied by comparison with the nuclear magnetic resonance solution structure of hirudin(1-51). J. Mol. Biol. 228:1992;1206-1211.
    • (1992) J. Mol. Biol. , vol.228 , pp. 1206-1211
    • Szyperski, T.1    Guntert, P.2    Stone, S.R.3    Tulinsky, A.4    Bode, W.5    Huber, R.6    Wuthrich, K.7
  • 26
    • 0032557503 scopus 로고    scopus 로고
    • Electrostatic enhancement of diffusion-controlled protein-protein association: Comparison of theory and experiment on barnase and barstar
    • Vijayakumar M., Wong K. Y., Schreiber G., Fersht A. R., Szabo A., Zhou H. Z. Electrostatic enhancement of diffusion-controlled protein-protein association: Comparison of theory and experiment on barnase and barstar. J. Mol. Biol. 278:1998;1015-1024.
    • (1998) J. Mol. Biol. , vol.278 , pp. 1015-1024
    • Vijayakumar, M.1    Wong, K.Y.2    Schreiber, G.3    Fersht, A.R.4    Szabo, A.5    Zhou, H.Z.6
  • 27
    • 0031012271 scopus 로고    scopus 로고
    • Very rapid, ionic strenght-dependent association and folding of a heterodimeric leucine zipper
    • Wendt H., Leder L., Harma H., Jelesarov I., Baice A., Bosshard H. R. Very rapid, ionic strenght-dependent association and folding of a heterodimeric leucine zipper. Biochemistry. 36:1997;204-213.
    • (1997) Biochemistry , vol.36 , pp. 204-213
    • Wendt, H.1    Leder, L.2    Harma, H.3    Jelesarov, I.4    Baice, A.5    Bosshard, H.R.6
  • 28
    • 0031547533 scopus 로고    scopus 로고
    • 15N Relaxation and structural studies reveal slow conformational exchange in barstar C40/82A
    • 15N Relaxation and structural studies reveal slow conformational exchange in barstar C40/82A. J. Mol. Biol. 268:1997;494-511.
    • (1997) J. Mol. Biol. , vol.268 , pp. 494-511
    • Wong, K.B.1    Fersht, A.R.2    Freund, S.M.V.3
  • 29
    • 0027161336 scopus 로고
    • Brownian dynamics study of the influences of electrostatic interaction and diffusion of protein-protein association kinetics
    • Zhou H. X. Brownian dynamics study of the influences of electrostatic interaction and diffusion of protein-protein association kinetics. Biophys. J. 64:1993;1711-1726.
    • (1993) Biophys. J. , vol.64 , pp. 1711-1726
    • Zhou, H.X.1
  • 30
    • 0030729719 scopus 로고    scopus 로고
    • Design of fast enzymes by optimizing interaction potential in active site
    • Zhou H. X., Wong K. Y., Vifayakumar M. Design of fast enzymes by optimizing interaction potential in active site. Proc. Natl Acad. Sci. USA. 94:1997;12372-12377.
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 12372-12377
    • Zhou, H.X.1    Wong, K.Y.2    Vifayakumar, M.3
  • 31
    • 0000827703 scopus 로고    scopus 로고
    • Effect of interaction potentials in diffusion-influenced reactions with small reactive regions
    • Zhou H.-Z. Effect of interaction potentials in diffusion-influenced reactions with small reactive regions. J. Chem. Phys. 105:1996;7235-7237.
    • (1996) J. Chem. Phys. , vol.105 , pp. 7235-7237
    • Zhou, H.-Z.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.