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Volumn 300, Issue 5, 2000, Pages 1335-1359

Amino acid conformational preferences and solvation of polar backbone atoms in peptides and proteins

Author keywords

Amino acid preferences; Electrostatic screening; Secondary structure; Solvation free energy

Indexed keywords

AMINO ACID; PEPTIDE; PROTEIN;

EID: 0034725551     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.2000.3901     Document Type: Article
Times cited : (59)

References (86)
  • 2
    • 0026723852 scopus 로고
    • Use of a potential of mean force to analyse free energy contributions in protein folding
    • (1992) Biochemistry , vol.31 , pp. 6290-6297
    • Avbelj, F.1
  • 4
    • 0032511138 scopus 로고    scopus 로고
    • Role of main-chain electrostatics, hydrophobic effect, and side-chain conformational entropy in determining the secondary structure of proteins
    • (1998) J. Mol. Biol. , vol.279 , pp. 665-684
    • Avbelj, F.1    Fele, L.2
  • 6
    • 0028960071 scopus 로고
    • Role of electrostatic screening in determining protein main chain conformational preferences
    • (1995) Biochemistry , vol.34 , pp. 755-764
    • Avbelj, F.1    Moult, J.2
  • 11
    • 0008019563 scopus 로고
    • Solvation Thermodynamics, Plenum Press, New York
    • (1987)
    • Ben-Naim, A.1
  • 12
    • 0025261918 scopus 로고
    • Solvent effects on protein association and protein folding
    • (1990) Biopolymers , vol.29 , pp. 567-596
    • Ben-Naim, A.1
  • 22
    • 0016352763 scopus 로고
    • Hydrophobic bonding and accessible surface area in proteins
    • (1974) Nature , vol.248 , pp. 338-339
    • Chothia, C.1
  • 23
    • 0016606973 scopus 로고
    • Structural invariants in protein folding
    • (1975) Nature , vol.254 , pp. 304-308
    • Chothia, C.1
  • 24
  • 25
    • 0015967881 scopus 로고
    • Conformational parameters for amino acid in helical, beta-sheet, and random coil regions calculated from proteins
    • (1974) Biochemistry , vol.13 , pp. 211-222
    • Chou, P.Y.1    Fasman, G.D.2
  • 31
    • 0031187388 scopus 로고    scopus 로고
    • Langevin dipoles model for ab initio calculations of chemical processes in solution: Parametrization and application to hydration free energies of neutral and ionic solutes and conformational analysis in aqueous solution
    • (1997) J. Phys. Chem. B , vol.101 , pp. 5583-5595
    • Florian, J.1    Warshel, A.2
  • 42
    • 0027411181 scopus 로고
    • Thermodynamic betasheet propensities measured using a zinc finger host peptide
    • (1993) Nature , vol.362 , pp. 267-270
    • Kim, C.A.1    Berg, J.M.2
  • 54
  • 56
    • 0031127043 scopus 로고    scopus 로고
    • Development of the multiple sequence approximation with the agadir model of α-helix formation
    • (1997) Biopolymers , vol.41 , pp. 495-509
    • Munoz, V.1    Serrano, L.2
  • 61
    • 0025222978 scopus 로고
    • A thermodynamics scale for the helix-forming tendencies of the commonly occurring amino acids
    • (1990) Science , vol.250 , pp. 646-651
    • O'Neal, K.T.1    DeGrado, W.F.2
  • 66
    • 0000574454 scopus 로고
    • Integral equation model for aqueous solvation of polyatomic solutes: Application to the determination of the free energy for the internal motion of biomolecules
    • (1986) J. Phys. Chem. , vol.90 , pp. 6335-6345
    • Pettitt, B.M.1    Karplus, M.2    Rossky, P.J.3
  • 70
    • 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. 389-404
    • Russell, S.T.1    Warshel, A.2
  • 71
    • 0000695923 scopus 로고
    • A cff91-based continuum solvation model: Solvation free energy of small organic molecules and conformations of the alanine dipeptide in solution
    • (1994) Mol. Simulation , vol.13 , pp. 347-365
    • Schmid, A.B.1    Fine, R.M.2
  • 77
    • 11744256643 scopus 로고
    • Molecular interactions in solution: An overview of methods based on continuous distributions of the solvent
    • (1994) Chem. Rev. , vol.94 , pp. 2027-2094
    • Tomasi, J.1    Persico, M.2
  • 78
    • 0029865495 scopus 로고    scopus 로고
    • Analysis of thermodynamic determinants in helix propensities of nonpolar amino acids through a novel free energy calculation
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 995-1001
    • Wang, J.1    Purisima, E.O.2
  • 81
    • 0025113815 scopus 로고
    • Helix-coil stability constants for the naturally occurring amino acids in water. XXIV. Half-cysteine parameters from random poly(hydroxybutylglutamine-co-S-methylthio-L-cysteine)
    • (1990) Biopolymers , vol.30 , pp. 121-134
    • Wojcik, J.1    Altmann, K.-H.2    Scheraga, H.A.3
  • 83
    • 0029150955 scopus 로고
    • Flee energy determinants of secondary structure formation: II. Anti-parallel β-sheets
    • (1995) J. Mol. Biol. , vol.252 , pp. 366-376
    • Yang, A.1    Honig, B.2
  • 85
    • 0030596522 scopus 로고    scopus 로고
    • Free energy determinants of secondary structure formation: III β-turns and their role in protein folding
    • (1996) J. Mol. Biol. , vol.259 , pp. 873-882
    • Yang, A.1    Honig, B.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.