메뉴 건너뛰기




Volumn 44, Issue 4, 2001, Pages 400-417

What are the dielectric "constants" of proteins and how to validate electrostatic models?

Author keywords

Electrostatic energies; Ion pairs in proteins; Protein dielectric constants; Self energy

Indexed keywords

PROTEIN;

EID: 0035451052     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/prot.1106     Document Type: Review
Times cited : (844)

References (101)
  • 2
    • 0000467270 scopus 로고
    • Electrostatic basis of structure-function correlation in proteins
    • (1981) Accts Chem Res , vol.14 , pp. 284-290
    • Warshel, A.1
  • 10
    • 0000414723 scopus 로고    scopus 로고
    • Electrostatic potential in rhodopseudomonas viridis reaction centers: Implications for the driving force and directionality of electron transfer
    • (1996) J Phys Chem , vol.100 , pp. 4277-4291
    • Gunner, M.1    Nichols, A.2    Honig, B.3
  • 11
    • 0344418714 scopus 로고    scopus 로고
    • Simulating proton translocations in proteins: Probing proton transfer pathways in the rhodobacter sphaeroides reaction center
    • (1999) Proteins , vol.36 , pp. 484-500
    • Sham, Y.1    Muegge, I.2    Warshel, A.3
  • 13
  • 15
    • 0026596911 scopus 로고
    • Calculations of antibody-antigen interactions: Microscopic and semi-microscopic evaluation of the free energies of binding of phosphorylcholine analogs to mcpc603
    • (1992) Prot Eng , vol.5 , pp. 215-228
    • Lee, F.S.1    Chu, Z.T.2    Bolger, M.B.3    Warshel, A.4
  • 19
    • 0022248941 scopus 로고
    • Calculations of electrostatic energies in proteins; the energetics of ionized groups in bovine pancreatic trypsin inhibitor
    • (1985) J Mol Biol , vol.185 , pp. 389
    • Russell, S.T.1    Warshel, A.2
  • 25
    • 0033012333 scopus 로고    scopus 로고
    • A self-consistent, microspcopic modulated screened coulomb potential approximation to calculate ph-dependent electrostatic effects in proteins
    • (1999) Biophys J , vol.75 , pp. 3-22
    • Mehler, E.L.1    Guarnieri, F.2
  • 31
    • 33744799306 scopus 로고    scopus 로고
    • The lorentz-debye-sack theory and dielectric screening of electrostatic effects in proteins and nucleic acids
    • Murray JS, Sen K, editors. Molecular electrostatic potentials. New York: Elsevier
    • (1996) , pp. 371-406
    • Mehler, E.L.1
  • 35
    • 0001382020 scopus 로고    scopus 로고
    • Calculation of absolute binding free energies for charged ligands and effects of long-range electrostatic interactions
    • (1996) J Comp Chem , vol.17 , pp. 1587
    • Åqvist, J.1
  • 37
    • 0019889036 scopus 로고
    • Calculations of enzymic reactions: Calculations of pka, proton transfer reactions, and general acid catalysis reactions in enzymes
    • (1981) Biochemistry , vol.20 , pp. 3167-3177
    • Warshel, A.1
  • 41
    • 0017100947 scopus 로고
    • Theoretical studies of enzymatic reactions: Dielectric, electrostatic and steric stabilization of the carbonium ion in the reaction of lysozyme
    • (1976) J Mol Biol , vol.103 , pp. 227-249
    • Warshel, A.1    Levitt, M.2
  • 42
    • 0000115003 scopus 로고
    • A local reaction field method for fast evaluation of long-range electrostatic interactions in molecular simulations
    • (1992) J Chem Phys , vol.97 , pp. 3100-3107
    • Lee, F.S.1    Warshel, A.2
  • 43
    • 7044239742 scopus 로고
    • Free energy calculations: Applications to chemical and biochemical phenomena
    • (1993) Chem Rev , vol.93 , pp. 2395-2417
    • Kollman, P.1
  • 44
  • 45
    • 0000320146 scopus 로고    scopus 로고
    • The surface constrained all atom model provides size independent results in calculations of hydration free energies
    • (1998) J Chem Phys , vol.109 , pp. 7940-7944
    • Sham, Y.Y.1    Warshel, A.2
  • 49
    • 20644431615 scopus 로고
    • Theory of solutions of molecules containing widely separated charges with special application to zwitterions
    • (1934) J Chem Phys , vol.2 , pp. 351-361
    • Kirkwood, J.G.1
  • 50
    • 0000652941 scopus 로고
    • Dielectric and thermodynamic response of generalized reaction field model for liquid state simulations
    • (1993) J Chem Phys , vol.99 , pp. 9847-9852
    • Alper, H.1    Levy, R.M.2
  • 51
  • 52
    • 36549094414 scopus 로고
    • A surface constrained all-atom solvent model for effective simulations of polar solutions
    • (1989) J Chem Phys , vol.91 , pp. 3647-3661
    • King, G.1    Warshel, A.2
  • 54
    • 0001655657 scopus 로고
    • Finite representation of an infinite bulk system: Solvent boundary potential for computer simulations
    • (1994) J Chem Phys , vol.100 , pp. 9050-9063
    • Beglov, D.1    Roux, B.2
  • 56
    • 0030996290 scopus 로고    scopus 로고
    • Control of reduction potential by protein matrix: Lesson from a spherical protein model
    • (1997) J Biol Inorg Chem , vol.2 , pp. 109-113
    • Zhou, H.X.1
  • 62
  • 63
    • 84986466995 scopus 로고
    • Microscopic models for quantum mechanical calculations of chemical processes in solutions: LD/AMPAC and SCAAS/AMPAC calculations of solvation energies
    • (1992) J Comp Chem , vol.13 , pp. 199
    • Luzhkov, V.1    Warshel, A.2
  • 78
    • 0001112223 scopus 로고
    • The inter-ionic attraction theory of ionized solutes. IV. The influence of variation of dielectric constant on the limiting law for small concentrations
    • (1925) J Am Chem Soc , vol.47 , pp. 2129-2134
    • Debye, P.J.W.1    Pauling, L.2
  • 79
    • 33947344144 scopus 로고
    • The free energy of hydration of ions and the electrostriction of the solvent
    • (1926) J Am Chem Soc , vol.48 , pp. 2589-2603
    • Webb, T.J.1
  • 80
    • 0003131896 scopus 로고
    • The electrostatic contribution to hindered rotation in certain ions and dipolar ions in solution III
    • (1944) J Chem Phys , vol.12 , pp. 56-61
    • Hill, T.L.1
  • 83
    • 0030945495 scopus 로고    scopus 로고
    • Incorporating protein conformational flexibility into the calculation of ph-dependent protein properties
    • (1997) Biophys J , vol.72 , pp. 2075
    • Alexov, E.1    Gunner, M.2
  • 91
    • 0015994218 scopus 로고
    • Real-space refinement of the structure of hen white lysozyme
    • (1974) J Mol Biol , vol.82 , pp. 371
    • Diamond, R.1
  • 99
    • 0032856161 scopus 로고    scopus 로고
    • Buried, charged, non-ion-paired aspartic acid 76 contributes favorably to the conformational stability of ribonuclease
    • (1999) Biochemistry , vol.38 , pp. 13379-13384
    • Giletto, A.1    Pace, C.N.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.