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Volumn 7, Issue 1, 1998, Pages 206-210

Computation of electrostatic complements to proteins: A case of charge stabilized binding

Author keywords

Continuum electrostatics; Electrostatic complement; Protein binding; Rational ligand design

Indexed keywords

ARTICLE; BINDING SITE; ELECTRICITY; LIGAND BINDING; MOLECULAR INTERACTION; PRIORITY JOURNAL; PROTEIN BINDING;

EID: 0031891022     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1002/pro.5560070122     Document Type: Article
Times cited : (64)

References (27)
  • 3
    • 0000682989 scopus 로고    scopus 로고
    • Finite difference Poisson-Boltzmann electrostatic calculations: Increased accuracy achieved by harmonic dielectric smoothing and charge antialiasing
    • Bruccoleri RE, Novotny J, Davis ME, Sharp KA. 1997. Finite difference Poisson-Boltzmann electrostatic calculations: Increased accuracy achieved by harmonic dielectric smoothing and charge antialiasing. J Comput Chem 18:268-276.
    • (1997) J Comput Chem , vol.18 , pp. 268-276
    • Bruccoleri, R.E.1    Novotny, J.2    Davis, M.E.3    Sharp, K.A.4
  • 4
    • 0024250301 scopus 로고
    • Polar hydrogen positions in proteins: Empirical energy placement and neutron diffraction comparison
    • Brünger AT, Karplus M. 1988. Polar hydrogen positions in proteins: Empirical energy placement and neutron diffraction comparison. Proteins Struct Funct Genet 4:148-156.
    • (1988) Proteins Struct Funct Genet , vol.4 , pp. 148-156
    • Brünger, A.T.1    Karplus, M.2
  • 5
    • 0028074974 scopus 로고
    • Protein-protein recognition: Crystal structure analysis of a barnase-barstar complex at 2.0-Å resolution
    • Buckle AM, Schreiber G, Fersht AR. 1994. Protein-protein recognition: Crystal structure 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
  • 6
    • 0023779259 scopus 로고
    • Calculation of the total electrostatic energy of a macromolecular system: Solvation energies, binding energies, and conformational analysis
    • Gilson MK, Honig B. 1988. Calculation of the total electrostatic energy of a macromolecular system: Solvation energies, binding energies, and conformational analysis. Proteins Struct Funct Genet 4:7-18.
    • (1988) Proteins Struct Funct Genet , vol.4 , pp. 7-18
    • Gilson, M.K.1    Honig, B.2
  • 7
    • 84988087911 scopus 로고
    • Calculating the electrostatic potential of molecules in solution: Method and error assessment
    • Gilson MK, Sharp KA, Honig BH. 1988. Calculating the electrostatic potential of molecules in solution: Method and error assessment. J Comput Chem 9:327-335.
    • (1988) J Comput Chem , vol.9 , pp. 327-335
    • Gilson, M.K.1    Sharp, K.A.2    Honig, B.H.3
  • 8
    • 0028204490 scopus 로고
    • Do salt bridges stabilize proteins? A continuum electrostatic analysis
    • Hendsch ZS, Tidor B. 1994. Do salt bridges stabilize proteins? A continuum electrostatic analysis. Protein Sci 3:211-226.
    • (1994) Protein Sci , vol.3 , pp. 211-226
    • Hendsch, Z.S.1    Tidor, B.2
  • 9
    • 0031165571 scopus 로고    scopus 로고
    • Optimization of electrostatic binding free energy
    • Lee L-P, Tidor B. 1997. Optimization of electrostatic binding free energy. J Chem Phys 106:8681-8690.
    • (1997) J Chem Phys , vol.106 , pp. 8681-8690
    • Lee, L.-P.1    Tidor, B.2
  • 10
    • 0030917740 scopus 로고    scopus 로고
    • Exceptionally stable salt bridges in cytochrome P450cam have functional roles
    • Lounnas V, Wade, RC. 1997. Exceptionally stable salt bridges in cytochrome P450cam have functional roles. Biochemistry 36:5402-5417.
    • (1997) Biochemistry , vol.36 , pp. 5402-5417
    • Lounnas, V.1    Wade, R.C.2
  • 11
    • 0028239626 scopus 로고
    • Salt effects on protein-DNA interactions: The λcI repressor and EcoRI endonuclease
    • Misra VK, Hecht JL, Sharp KA, Friedman RA, Honig B. 1994a. Salt effects on protein-DNA interactions: The λcI repressor and EcoRI endonuclease. J Mol Biol 238:264-280.
    • (1994) J Mol Biol , vol.238 , pp. 264-280
    • Misra, V.K.1    Hecht, J.L.2    Sharp, K.A.3    Friedman, R.A.4    Honig, B.5
  • 12
    • 0028246710 scopus 로고
    • Salt effects on ligand-DNA binding: Minor groove binding antibiotics
    • Misra VK, Sharp KA, Friedman RA, Honig B. 1994b. Salt effects on ligand-DNA binding: Minor groove binding antibiotics. J Mol Biol 238: 245-263.
    • (1994) J Mol Biol , vol.238 , pp. 245-263
    • Misra, V.K.1    Sharp, K.A.2    Friedman, R.A.3    Honig, B.4
  • 13
    • 0031547977 scopus 로고    scopus 로고
    • Empirical free energy calculations: A blind test and further improvements to the method
    • Novotny J, Bruccoleri RE, Davis M, Sharp KA. 1997. Empirical free energy calculations: A blind test and further improvements to the method. J Mol Biol 265:401-411.
    • (1997) J Mol Biol , vol.265 , pp. 401-411
    • Novotny, J.1    Bruccoleri, R.E.2    Davis, M.3    Sharp, K.A.4
  • 14
    • 0026438116 scopus 로고
    • Electrostatic fields in antibodies and antibody/ antigen complexes
    • Novotny J, Sharp K. 1992. Electrostatic fields in antibodies and antibody/ antigen complexes. Prog Biophys Mol Biol 58:203-224.
    • (1992) Prog Biophys Mol Biol , vol.58 , pp. 203-224
    • Novotny, J.1    Sharp, K.2
  • 15
    • 0020482656 scopus 로고
    • Building models of globular protein molecules from their amino acid sequences. I. Theory
    • Paul CH. 1982. Building models of globular protein molecules from their amino acid sequences. I. Theory. J Mol Biol 155:53-62.
    • (1982) J Mol Biol , vol.155 , pp. 53-62
    • Paul, C.H.1
  • 17
    • 0030606788 scopus 로고    scopus 로고
    • Electrostatic interactions in hirudin-thrombin binding
    • Sharp KA. 1996. Electrostatic interactions in hirudin-thrombin binding. Biophys Chem 61:31-49.
    • (1996) Biophys Chem , vol.61 , pp. 31-49
    • Sharp, K.A.1
  • 18
    • 0025283002 scopus 로고
    • Electrostatic interactions in macromolecules: Theory and applications
    • Sharp KA, Honig B. 1990. Electrostatic interactions in macromolecules: Theory and applications. Annu Rev Biophys Biophys Chem 19:301-332.
    • (1990) Annu Rev Biophys Biophys Chem , vol.19 , pp. 301-332
    • Sharp, K.A.1    Honig, B.2
  • 19
    • 0001620364 scopus 로고    scopus 로고
    • Electrostatic binding energy calculation using the finite difference solution to the linearized Poisson-Boltzmann equation: Assessment of its accuracy
    • Shen J, Wendoloski J. 1996. Electrostatic binding energy calculation using the finite difference solution to the linearized Poisson-Boltzmann equation: Assessment of its accuracy. J Comput Chem 17:350-357.
    • (1996) J Comput Chem , vol.17 , pp. 350-357
    • Shen, J.1    Wendoloski, J.2
  • 20
    • 32844457567 scopus 로고
    • Accurate calculation of hydration free energies using macroscopic solvent models
    • Sitkoff D, Sharp KA, Honig B. 1994. Accurate calculation of hydration free energies using macroscopic solvent models. J Phys Chem 95:1978-1988.
    • (1994) J Phys Chem , vol.95 , pp. 1978-1988
    • Sitkoff, D.1    Sharp, K.A.2    Honig, B.3
  • 21
    • 0004203940 scopus 로고
    • Wellesley, Massachusetts: Wellesley-Cambridge Press
    • Strang G. 1993. Introduction to linear algebra. Wellesley, Massachusetts: Wellesley-Cambridge Press.
    • (1993) Introduction to Linear Algebra
    • Strang, G.1
  • 22
    • 0001415860 scopus 로고
    • The role of the α-helix in the structure of proteins. Optical rotatory dispersion of β-lactoglobulin
    • Tanford C, De PK, Taggart VG. 1960. The role of the α-helix in the structure of proteins. Optical rotatory dispersion of β-lactoglobulin. J Am Chem Soc 82:6028-6034.
    • (1960) J Am Chem Soc , vol.82 , pp. 6028-6034
    • Tanford, C.1    De, P.K.2    Taggart, V.G.3
  • 23
    • 0029564595 scopus 로고
    • Are buried salt bridges important for protein stability and conformational specificity?
    • Waldburger CD, Schildbach JF, Sauer RT. 1995. Are buried salt bridges important for protein stability and conformational specificity? Nat Struct Biol 2:122-128.
    • (1995) Nat Struct Biol , vol.2 , pp. 122-128
    • Waldburger, C.D.1    Schildbach, J.F.2    Sauer, R.T.3
  • 24
    • 0030271002 scopus 로고    scopus 로고
    • Energetic decomposition of the α-helix-coil equilibrium of a dynamic model system
    • Wang L, O'Connell T, Tropsha A, Hermans J. 1996. Energetic decomposition of the α-helix-coil equilibrium of a dynamic model system. Biopolymers 39:479-489.
    • (1996) Biopolymers , vol.39 , pp. 479-489
    • Wang, L.1    O'Connell, T.2    Tropsha, A.3    Hermans, J.4
  • 25
    • 0029864591 scopus 로고    scopus 로고
    • Direct measurement of salt-bridge solvation energies using a peptide model system: Implications for protein stability
    • Wimley WC, Gawrisch K, Creamer TP, White SH. 1996. Direct measurement of salt-bridge solvation energies using a peptide model system: Implications for protein stability. Proc Natl Acad Sci USA 93:2985-2990.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 2985-2990
    • Wimley, W.C.1    Gawrisch, K.2    Creamer, T.P.3    White, S.H.4
  • 26
    • 0031561809 scopus 로고    scopus 로고
    • Protein binding versus protein folding: The role of hydrophilic bridges in protein associations
    • Xu D, Lin SL, Nussinov R. 1997. Protein binding versus protein folding: The role of hydrophilic bridges in protein associations. J Mol Biol 265: 68-84.
    • (1997) J Mol Biol , vol.265 , pp. 68-84
    • Xu, D.1    Lin, S.L.2    Nussinov, R.3
  • 27
    • 0029121068 scopus 로고
    • Free energy determinants of secondary structure formation: I. α-helices
    • Yang A-S, Honig B. 1995. Free energy determinants of secondary structure formation: I. α-helices. J Mol Biol 252:351-365.
    • (1995) J Mol Biol , vol.252 , pp. 351-365
    • Yang, A.-S.1    Honig, B.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.