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Volumn 14, Issue 7, 2005, Pages 1772-1777

Protein flexibility prediction by an all-atom mean-field statistical theory

Author keywords

All atom model; Mean field statistical theory; Protein flexibility; Protein thermodynamics

Indexed keywords

FODRIN; PROTEIN; PROTEIN SH3; STAPHYLOCOCCUS PROTEIN A; UNCLASSIFIED DRUG;

EID: 22244439241     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.041311005     Document Type: Article
Times cited : (18)

References (20)
  • 2
    • 0030623823 scopus 로고    scopus 로고
    • Direct evaluation of thermal fluctuations in proteins using a single parameter harmonic potential
    • Bahar, I., Atilgan, A.R., and Erman, B. 1997. Direct evaluation of thermal fluctuations in proteins using a single parameter harmonic potential. Fold. Des. 2: 173-181.
    • (1997) Fold. Des. , vol.2 , pp. 173-181
    • Bahar, I.1    Atilgan, A.R.2    Erman, B.3
  • 5
    • 0036904038 scopus 로고    scopus 로고
    • Changes in flexibility upon binding: Application of the self-consistent pair contact probability method to protein-protein interactions
    • Canino, L.S., Shen, T.Y., and McCammon, J.A. 2002. Changes in flexibility upon binding: Application of the self-consistent pair contact probability method to protein-protein interactions. J. Chem. Phys. 117: 9927-9933.
    • (2002) J. Chem. Phys. , vol.117 , pp. 9927-9933
    • Canino, L.S.1    Shen, T.Y.2    McCammon, J.A.3
  • 6
    • 0030877077 scopus 로고    scopus 로고
    • Extent and nature of contacts between protein molecules in crystal lattices and between subunits of protein oligomers
    • Dasgupta, S., Iyer, G.H., Lawrence, S.H., and Bell, J.A. 1997. Extent and nature of contacts between protein molecules in crystal lattices and between subunits of protein oligomers. Proteins 28: 494-514.
    • (1997) Proteins , vol.28 , pp. 494-514
    • Dasgupta, S.1    Iyer, G.H.2    Lawrence, S.H.3    Bell, J.A.4
  • 7
    • 0034663710 scopus 로고    scopus 로고
    • Dynamics of proteins predicted by molecular dynamics simulations and analytical approaches: Application to α-amylase inhibitor
    • Doruker, P., Atilgan, A.R., and Bahar, I. 2000. Dynamics of proteins predicted by molecular dynamics simulations and analytical approaches: Application to α-amylase inhibitor. Proteins 40: 512-524.
    • (2000) Proteins , vol.40 , pp. 512-524
    • Doruker, P.1    Atilgan, A.R.2    Bahar, I.3
  • 8
    • 0035427398 scopus 로고    scopus 로고
    • Protein flexibility prediction using graph theory
    • Jacobs, D.J., Rader, A.J., Kuhn, L.A., and Thorpe, M.F. 2001. Protein flexibility prediction using graph theory. Proteins 44: 150-165.
    • (2001) Proteins , vol.44 , pp. 150-165
    • Jacobs, D.J.1    Rader, A.J.2    Kuhn, L.A.3    Thorpe, M.F.4
  • 9
    • 0042130544 scopus 로고    scopus 로고
    • Simple two-state protein folding kinetics requires near-Levinthal thermodynamic cooperativity
    • Kaya, H. and Chan, H. 2003. Simple two-state protein folding kinetics requires near-Levinthal thermodynamic cooperativity. Proteins 52: 510-523.
    • (2003) Proteins , vol.52 , pp. 510-523
    • Kaya, H.1    Chan, H.2
  • 10
    • 0037452894 scopus 로고    scopus 로고
    • Discrimination of native protein structures using atom-atom contact scoring
    • McConkey, B.J., Sobolev, V., and Eldman, M. 2003. Discrimination of native protein structures using atom-atom contact scoring. Proc. Natl. Acad. Sci. 100: 3215-3220.
    • (2003) Proc. Natl. Acad. Sci. , vol.100 , pp. 3215-3220
    • McConkey, B.J.1    Sobolev, V.2    Eldman, M.3
  • 12
    • 0036073320 scopus 로고    scopus 로고
    • Crucial stages of protein folding through a solvable model: Predicting target sites for enzyme-inhibiting drugs
    • Micheletti, C., Cecconi, F., Flammini, A., and Maritan, A. 2002. Crucial stages of protein folding through a solvable model: Predicting target sites for enzyme-inhibiting drugs. Protein Sci. 11: 1878-1887.
    • (2002) Protein Sci. , vol.11 , pp. 1878-1887
    • Micheletti, C.1    Cecconi, F.2    Flammini, A.3    Maritan, A.4
  • 13
    • 2442543557 scopus 로고    scopus 로고
    • Accurate and efficient description of protein vibrational dynamics: Comparing molecular dynamics and Gaussian models
    • Micheletti, C., Carloni, P., and Maritan, A. 2004. Accurate and efficient description of protein vibrational dynamics: Comparing molecular dynamics and Gaussian models. Proteins 55: 635-645.
    • (2004) Proteins , vol.55 , pp. 635-645
    • Micheletti, C.1    Carloni, P.2    Maritan, A.3
  • 14
    • 33845377127 scopus 로고
    • Estimation of effective interresidue contact energies from protein crystal structures: Quasi-chemical approximation
    • Miyazawa, S. and Jernigan, R. 1985. Estimation of effective interresidue contact energies from protein crystal structures: Quasi-chemical approximation. Macromole 18: 534-552.
    • (1985) Macromole , vol.18 , pp. 534-552
    • Miyazawa, S.1    Jernigan, R.2
  • 15
    • 0018588511 scopus 로고
    • Stability of proteins: Small globular proteins
    • Privalov, P.L. 1979. Stability of proteins: Small globular proteins. Adv. Protein Chem. 33: 167-241.
    • (1979) Adv. Protein Chem. , vol.33 , pp. 167-241
    • Privalov, P.L.1
  • 16
    • 0037025564 scopus 로고    scopus 로고
    • Unfolding proteins under external forces: A solvable model under the self-consistent pair contact probability approximation
    • Shen, T., Canino, L.S., and McCammon, J.A. 2002. Unfolding proteins under external forces: A solvable model under the self-consistent pair contact probability approximation. Phys. Rev. Lett. 89: 068103.
    • (2002) Phys. Rev. Lett. , vol.89 , pp. 068103
    • Shen, T.1    Canino, L.S.2    McCammon, J.A.3
  • 17
    • 0016696599 scopus 로고
    • Studies on protein folding, unfolding and fluctuations by computer simulations
    • Taketomi, H., Ueda, Y., and Go, N. 1975. Studies on protein folding, unfolding and fluctuations by computer simulations. Int. J. Peptide Protein Res. 7: 445-459.
    • (1975) Int. J. Peptide Protein Res. , vol.7 , pp. 445-459
    • Taketomi, H.1    Ueda, Y.2    Go, N.3
  • 18
    • 0017842051 scopus 로고
    • Studies on protein folding, unfolding and fluctuations by computer simulations, II: A three-dimensional lattice model of lysozyme
    • Ueda, Y., Taketomi, H., and Go, N. 1978. Studies on protein folding, unfolding and fluctuations by computer simulations, II: A three-dimensional lattice model of lysozyme. Biopolymers 17: 1531-1548.
    • (1978) Biopolymers , vol.17 , pp. 1531-1548
    • Ueda, Y.1    Taketomi, H.2    Go, N.3
  • 19
    • 0037075457 scopus 로고    scopus 로고
    • Thermodynamics of an all-atom off-lattice model of the fragment B of staphylococcal protein A: Implication for the origin of the cooperativity of protein folding
    • Zhou, Y. and Linhananta, A. 2002. Thermodynamics of an all-atom off-lattice model of the fragment B of staphylococcal protein A: Implication for the origin of the cooperativity of protein folding. J. Phys. Chem. B 106: 1481-1485.
    • (2002) J. Phys. Chem. B , vol.106 , pp. 1481-1485
    • Zhou, Y.1    Linhananta, A.2
  • 20
    • 0032902402 scopus 로고    scopus 로고
    • The calorimetric criterion for a two-state process revisited
    • Zhou, Y., Hall, C.K., and Karplus, M. 1999. The calorimetric criterion for a two-state process revisited. Protein Sci. 8: 1064-1074.
    • (1999) Protein Sci. , vol.8 , pp. 1064-1074
    • Zhou, Y.1    Hall, C.K.2    Karplus, M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.