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Volumn 90, Issue 6, 2006, Pages 1913-1924

Diffusional encounter of barnase and barstar

Author keywords

[No Author keywords available]

Indexed keywords

BARNASE; BARSTAR; BACILLUS AMYLOLIQUEFACIENS RIBONUCLEASE; BACTERIAL PROTEIN; BARSTAR PROTEIN, BACILLUS AMYLOLIQUEFACIENS; ENZYME INHIBITOR; MULTIPROTEIN COMPLEX; RIBONUCLEASE;

EID: 33646005543     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1529/biophysj.105.075507     Document Type: Article
Times cited : (116)

References (33)
  • 1
    • 0033167137 scopus 로고    scopus 로고
    • On the protein-protein diffusional encounter complex
    • Gabdoulline, R. R., and R. C. Wade. 1999. On the protein-protein diffusional encounter complex. J. Mol. Recognit. 12:226-234.
    • (1999) J. Mol. Recognit. , vol.12 , pp. 226-234
    • Gabdoulline, R.R.1    Wade, R.C.2
  • 2
    • 0036468995 scopus 로고    scopus 로고
    • Kinetic studies of protein-protein interactions
    • Schreiber, G. 2002. Kinetic studies of protein-protein interactions. Curr. Opin. Struct. Biol. 12:41-47.
    • (2002) Curr. Opin. Struct. Biol. , vol.12 , pp. 41-47
    • Schreiber, G.1
  • 3
    • 0035830963 scopus 로고    scopus 로고
    • Protein-protein association: Investigation of factors influencing association rates by Brownian Dynamics simulation
    • Gabdoulline, R. R., and R. C. Wade. 2001. Protein-protein association: investigation of factors influencing association rates by Brownian Dynamics simulation. J. Mol. Biol. 306:1139-1155.
    • (2001) J. Mol. Biol. , vol.306 , pp. 1139-1155
    • Gabdoulline, R.R.1    Wade, R.C.2
  • 4
    • 0029873697 scopus 로고    scopus 로고
    • Rapid, electrostatically assisted association of proteins
    • Schreiber, G., and A. R. Fersht. 1996. Rapid, electrostatically assisted association of proteins. Nat. Struct. Biol. 3:427-431.
    • (1996) Nat. Struct. Biol. , vol.3 , pp. 427-431
    • Schreiber, G.1    Fersht, A.R.2
  • 5
    • 0029056922 scopus 로고
    • Energetics of protein-protein interactions: Analysis of the barnase-barstar interface by single mutations and double mutant cycles
    • Schreiber, G., and A. R. Fersht. 1995. Energetics of protein-protein interactions: analysis of the barnase-barstar interface by single mutations and double mutant cycles. J. Mol. Biol. 248:478-486.
    • (1995) J. Mol. Biol. , vol.248 , pp. 478-486
    • Schreiber, G.1    Fersht, A.R.2
  • 6
    • 0028074974 scopus 로고
    • Protein-protein recognition: Crystal structural analysis of a barnase-barstar complex at 2.0-Å resolution
    • Buckle, A. M., G. Schreiber, and A. R. Fersht. 1994. Protein-protein recognition: crystal structural analysis of a barnase-barstar complex at 2.0-Å resolution. Biochemistry. 33:8878-8889.
    • (1994) Biochemistry , vol.33 , pp. 8878-8889
    • Buckle, A.M.1    Schreiber, G.2    Fersht, A.R.3
  • 7
    • 0033605858 scopus 로고    scopus 로고
    • Predicting the rate enhancement of protein complex formation from the electrostatic energy of interaction
    • Selzer, T., and G. Schreiber. 1999. Predicting the rate enhancement of protein complex formation from the electrostatic energy of interaction. J. Mol. Biol. 287:409-419.
    • (1999) J. Mol. Biol. , vol.287 , pp. 409-419
    • Selzer, T.1    Schreiber, G.2
  • 8
    • 0032557503 scopus 로고    scopus 로고
    • Electrostatic enhancement of diffusion-controlled protein-protein association: Comparison of theory and experiment on barnase and barstar
    • Vijayakumar, M., K. Y. Wong, G. Schreiber, A. R. Fersht, A. Szabo, and H. Z. Zhou. 1998. Electrostatic enhancement of diffusion-controlled protein-protein association: comparison of theory and experiment on barnase and barstar. J. Mol. Biol. 278:1015-1024.
    • (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
  • 9
    • 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
  • 10
    • 4444301075 scopus 로고    scopus 로고
    • How optimal are the binding energetics of barnase and barstar
    • Wang, T., S. Tomic, R. R. Gabdoulline, and R. C. Wade. 2004. How optimal are the binding energetics of barnase and barstar. Biophys. J. 87:1618-1630.
    • (2004) Biophys. J. , vol.87 , pp. 1618-1630
    • Wang, T.1    Tomic, S.2    Gabdoulline, R.R.3    Wade, R.C.4
  • 11
    • 0032981961 scopus 로고    scopus 로고
    • Free energy landscapes of encounter complexes in protein-protein association
    • Camacho, C. J., Z. Weng, S. Vajda, and C. DeLisi. 1999. Free energy landscapes of encounter complexes in protein-protein association. Biophys. J. 76:1166-1178.
    • (1999) Biophys. J. , vol.76 , pp. 1166-1178
    • Camacho, C.J.1    Weng, Z.2    Vajda, S.3    DeLisi, C.4
  • 12
    • 0003187567 scopus 로고    scopus 로고
    • The atomic structure of protein-protein recognition sites
    • Conte, L. L., C. Chothia, and J. Janin. 1999. The atomic structure of protein-protein recognition sites. J. Mol. Biol. 285:2177-2198.
    • (1999) J. Mol. Biol. , vol.285 , pp. 2177-2198
    • Conte, L.L.1    Chothia, C.2    Janin, J.3
  • 13
    • 0038650855 scopus 로고    scopus 로고
    • Comparison of calculation and experiment implicates significant electrostatic contributions to the binding stability of barnase and barstar
    • Dong, F., M. Vaijayakumar, and H.-X. Zhou. 2003. Comparison of calculation and experiment implicates significant electrostatic contributions to the binding stability of barnase and barstar. Biophys. J. 85:49-60.
    • (2003) Biophys. J. , vol.85 , pp. 49-60
    • Dong, F.1    Vaijayakumar, M.2    Zhou, H.-X.3
  • 14
    • 0026723477 scopus 로고
    • Effect of active site residues in barnase on activity and stability
    • Meiering, E. M., L. Serrano, and A. R. Fersht. 1992. Effect of active site residues in barnase on activity and stability. J. Mol. Biol. 225:585-589.
    • (1992) J. Mol. Biol. , vol.225 , pp. 585-589
    • Meiering, E.M.1    Serrano, L.2    Fersht, A.R.3
  • 15
    • 33646200644 scopus 로고    scopus 로고
    • Free energy landscape of proteinprotein encounter resulting from Brownian Dynamics simulations of barnase:barstar
    • Spaar, A., and V. Helms. 2005. Free energy landscape of proteinprotein encounter resulting from Brownian Dynamics simulations of barnase:barstar. J. Chem. Theory Comput. 1:723-736.
    • (2005) J. Chem. Theory Comput. , vol.1 , pp. 723-736
    • Spaar, A.1    Helms, V.2
  • 16
    • 0037346726 scopus 로고    scopus 로고
    • The physics and bioinformatics of binding and folding-an energy landscape perspective
    • Papoian, G. A., and P. G. Wolynes. 2003. The physics and bioinformatics of binding and folding-an energy landscape perspective. Biopolymers. 68:333-349.
    • (2003) Biopolymers , vol.68 , pp. 333-349
    • Papoian, G.A.1    Wolynes, P.G.2
  • 17
    • 0033056708 scopus 로고    scopus 로고
    • Folding funnels, binding funnels, and protein function
    • Tsai, C.-J., S. Kumar, B. Ma, and R. Nussinov. 1999. Folding funnels, binding funnels, and protein function. Protein Sci. 8:1181-1190.
    • (1999) Protein Sci. , vol.8 , pp. 1181-1190
    • Tsai, C.-J.1    Kumar, S.2    Ma, B.3    Nussinov, R.4
  • 18
    • 9244244155 scopus 로고    scopus 로고
    • Transition state and encounter complex for fast association of cytochrome c2 with bacterial reaction center
    • Miyashita, O., J. N. Onuchic, and M. Y. Okamura. 2004. Transition state and encounter complex for fast association of cytochrome c2 with bacterial reaction center. Proc. Natl. Acad. Sci. USA. 101:16174-16179.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 16174-16179
    • Miyashita, O.1    Onuchic, J.N.2    Okamura, M.Y.3
  • 20
    • 85030607462 scopus 로고    scopus 로고
    • Reference deleted in proof
    • Reference deleted in proof.
  • 21
    • 0026124585 scopus 로고
    • Electrostatic and diffusion of molecules in solution: Simulations with the University-of-Houston-Brownian Dynamics program
    • Davis, M. E., J. D. Madura, B. A. Luty, and J. A. McCammon. 1991. Electrostatic and diffusion of molecules in solution: simulations with the University-of-Houston-Brownian Dynamics program. Comput. Phys. Commun. 62:187-197.
    • (1991) Comput. Phys. Commun. , vol.62 , pp. 187-197
    • Davis, M.E.1    Madura, J.D.2    Luty, B.A.3    McCammon, J.A.4
  • 22
    • 33645941402 scopus 로고
    • The OPLS potential functions for proteins, energy minimizations for crystals of cyclic peptides and crambin
    • Jorgensen, W. L., and J. Tirado-Rives. 1988. The OPLS potential functions for proteins, energy minimizations for crystals of cyclic peptides and crambin. J. Am. Chem. Soc. 110:1657-1666.
    • (1988) J. Am. Chem. Soc. , vol.110 , pp. 1657-1666
    • Jorgensen, W.L.1    Tirado-Rives, J.2
  • 23
    • 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
  • 24
    • 33845282908 scopus 로고
    • Electrostatic effects in the Brownian dynamics of association and orientation of heme proteins
    • Northrup, 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
    • Northrup, S.H.1    Boles, J.O.2    Reynolds, J.C.L.3
  • 25
    • 0344500752 scopus 로고    scopus 로고
    • Computer simulation of protein-protein association kinetics: Acetylcholinesterase-fasciculin
    • Elcock, A. H., R. R. Gabdoulline, R. C. Wade, and J. A. McCammon. 1999. Computer simulation of protein-protein association kinetics: acetylcholinesterase-fasciculin. J. Mol. Biol. 291:149-162.
    • (1999) J. Mol. Biol. , vol.291 , pp. 149-162
    • Elcock, A.H.1    Gabdoulline, R.R.2    Wade, R.C.3    McCammon, J.A.4
  • 26
    • 0031714012 scopus 로고    scopus 로고
    • Brownian dynamics simulation of protein-protein diffusional encounter
    • Gabdoulline, R. R., and R. C. Wade. 1998. Brownian dynamics simulation of protein-protein diffusional encounter. Methods. 14:329-341.
    • (1998) Methods , vol.14 , pp. 329-341
    • Gabdoulline, R.R.1    Wade, R.C.2
  • 27
    • 33750652614 scopus 로고
    • Brownian dynamics with hydrodynamic interactions
    • Ermak, D. L., and J. A. McCammon. 1978. Brownian dynamics with hydrodynamic interactions. J. Chem. Phys. 69:1352-1360.
    • (1978) J. Chem. Phys. , vol.69 , pp. 1352-1360
    • Ermak, D.L.1    McCammon, J.A.2
  • 28
    • 0030030147 scopus 로고    scopus 로고
    • Orientational steering in enzyme-substrate association: Ionic strength dependence of hydrodynamic torque effects
    • Antosiewicz, J., J. M. Briggs, and J. A. McCammon. 1996. Orientational steering in enzyme-substrate association: ionic strength dependence of hydrodynamic torque effects. Eur. Biophys. J. 24:137-141.
    • (1996) Eur. Biophys. J. , vol.24 , pp. 137-141
    • Antosiewicz, J.1    Briggs, J.M.2    McCammon, J.A.3
  • 29
    • 3142735054 scopus 로고    scopus 로고
    • Brownian Dynamics simulations of simplified cytochrome c molecules in the presence of a charged surface
    • Gorba, C., T. Geyer, and V. Helms. 2004. Brownian Dynamics simulations of simplified cytochrome c molecules in the presence of a charged surface. J. Chem. Phys. 121:457-464.
    • (2004) J. Chem. Phys. , vol.121 , pp. 457-464
    • Gorba, C.1    Geyer, T.2    Helms, V.3
  • 30
    • 3042814575 scopus 로고    scopus 로고
    • A Brownian Dynamics study: The effect of a membrane environment on an electron transfer system
    • Flöck, D., and V. Helms. 2004. A Brownian Dynamics study: the effect of a membrane environment on an electron transfer system. Biophys. J. 87:65-74.
    • (2004) Biophys. J. , vol.87 , pp. 65-74
    • Flöck, D.1    Helms, V.2
  • 31
    • 0001229341 scopus 로고    scopus 로고
    • Calculation of hydrodynamic properties of globular proteins from their atomic-level structure
    • de la Torre, J. G., M. L. Huertas, and B. Carrasco. 2000. Calculation of hydrodynamic properties of globular proteins from their atomic-level structure. Biophys. J. 78:719-730.
    • (2000) Biophys. J. , vol.78 , pp. 719-730
    • De La Torre, J.G.1    Huertas, M.L.2    Carrasco, B.3
  • 32
    • 0036923838 scopus 로고    scopus 로고
    • Brownian Dynamics simulation of rigid particles of arbitrary shape in external fields
    • Fernandes, M. X., and J. G. de la Torre. 2002. Brownian Dynamics simulation of rigid particles of arbitrary shape in external fields. Biophys. J. 83:3039-3048.
    • (2002) Biophys. J. , vol.83 , pp. 3039-3048
    • Fernandes, M.X.1    De La Torre, J.G.2


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