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Volumn 78, Issue 4, 2000, Pages 1665-1671

Theoretical studies of the response of a protein structure to cavity- creating mutations

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID SUBSTITUTION; ARTICLE; CHEMICAL BOND; ENERGY; MOLECULAR DYNAMICS; MUTATION; PROTEIN INTERACTION; PROTEIN STABILITY; PROTEIN STRUCTURE; STEREOSPECIFICITY;

EID: 0034106349     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(00)76718-X     Document Type: Article
Times cited : (23)

References (26)
  • 2
    • 0031127502 scopus 로고    scopus 로고
    • Protein hinge bending as seen in molecular dynamics simulations of native and M6I mutant T4 lysozymes
    • Arnold, G. E., and R. L. Ornstein. 1997. Protein hinge bending as seen in molecular dynamics simulations of native and M6I mutant T4 lysozymes. Biopolymers. 41:533-544.
    • (1997) Biopolymers , vol.41 , pp. 533-544
    • Arnold, G.E.1    Ornstein, R.L.2
  • 4
    • 0032080528 scopus 로고    scopus 로고
    • Domain motions in bacteriophage T4 lysozyme: A comparison between molecular dynamics and crystallographic data
    • de Groot, B. L., S. Hayward, D. M. F. van Aalten, A. Amadei, and H. J. C. Berendsen. 1998. Domain motions in bacteriophage T4 lysozyme: a comparison between molecular dynamics and crystallographic data. Proteins Struct. Funct. Genet. 31:116-127.
    • (1998) Proteins Struct. Funct. Genet. , vol.31 , pp. 116-127
    • De Groot, B.L.1    Hayward, S.2    Van Aalten, D.M.F.3    Amadei, A.4    Berendsen, H.J.C.5
  • 5
    • 0025370815 scopus 로고
    • Dominant forces in protein folding
    • Dill, K. A. 1990. Dominant forces in protein folding. Biochemistry. 29: 7133-7155.
    • (1990) Biochemistry , vol.29 , pp. 7133-7155
    • Dill, K.A.1
  • 6
    • 0027394606 scopus 로고
    • Similar hydrophobic replacements of Leu99 and Phe153 within the core of T4-lysozyme have different structural and thermodynamic consequences
    • Eriksson, A. E., W. A. Baase, and B. W. Matthews. 1993. Similar hydrophobic replacements of Leu99 and Phe153 within the core of T4-lysozyme have different structural and thermodynamic consequences. J. Mol. Biol. 229:747-769.
    • (1993) J. Mol. Biol. , vol.229 , pp. 747-769
    • Eriksson, A.E.1    Baase, W.A.2    Matthews, B.W.3
  • 7
    • 0026567907 scopus 로고
    • Response of a protein structure to cavity-creating mutations and its relation to the hydrophobic effect
    • Eriksson, A. E., W. A. Baase, X. J. Zhang, D. W. Heinz, M. Blaber, E. P. Baldwin, and B. W. Matthews. 1992. Response of a protein structure to cavity-creating mutations and its relation to the hydrophobic effect. Science. 255:178-183.
    • (1992) Science , vol.255 , pp. 178-183
    • Eriksson, A.E.1    Baase, W.A.2    Zhang, X.J.3    Heinz, D.W.4    Blaber, M.5    Baldwin, E.P.6    Matthews, B.W.7
  • 8
    • 0025047629 scopus 로고
    • T4 lysozyme displays five different crystal conformations
    • Faber. H. R., and B. W. Matthews. 1990. T4 lysozyme displays five different crystal conformations. Nature. 348:263-266.
    • (1990) Nature , vol.348 , pp. 263-266
    • Faber, H.R.1    Matthews, B.W.2
  • 10
    • 0024295240 scopus 로고
    • Contribution of hydrophobic interactions to protein stability
    • Kellis, J. T., K. Nyberg, D. Sali, and A. R. Fersht. 1988. Contribution of hydrophobic interactions to protein stability. Nature. 333:784-786.
    • (1988) Nature , vol.333 , pp. 784-786
    • Kellis, J.T.1    Nyberg, K.2    Sali, D.3    Fersht, A.R.4
  • 11
    • 0023741058 scopus 로고
    • Hydrophobic stabilization in T4 lysozyme determined directly by multiple substitutions of Ile 3
    • Matsumura, M., W. J. Becktel, and B. W. Matthews. 1988. Hydrophobic stabilization in T4 lysozyme determined directly by multiple substitutions of Ile 3. Nature. 334:406-410.
    • (1988) Nature , vol.334 , pp. 406-410
    • Matsumura, M.1    Becktel, W.J.2    Matthews, B.W.3
  • 12
    • 0346436100 scopus 로고
    • The three-dimensional structure of the lysozyme from bacteriophage T4
    • Matthews, B. W., and S. J. Remington. 1974. The three-dimensional structure of the lysozyme from bacteriophage T4. Proc. Nat. Acad. Sci. USA. 71:4178-4182.
    • (1974) Proc. Nat. Acad. Sci. USA , vol.71 , pp. 4178-4182
    • Matthews, B.W.1    Remington, S.J.2
  • 14
    • 1842326248 scopus 로고    scopus 로고
    • Conformation of T4 lysozyme in solution: Hinge-bending motion and the substrate-induced conformational transition studied by site-directed spin labeling
    • McHaourab, H. S., K. J. Oh, C. J. Fang, and W. L. Hubbell. 1997. Conformation of T4 lysozyme in solution: hinge-bending motion and the substrate-induced conformational transition studied by site-directed spin labeling. Biochemistry. 36:307-316.
    • (1997) Biochemistry , vol.36 , pp. 307-316
    • McHaourab, H.S.1    Oh, K.J.2    Fang, C.J.3    Hubbell, W.L.4
  • 15
    • 0029926518 scopus 로고    scopus 로고
    • Dynamics of proteins in different solvent systems: Analysis of essential motion in lipases
    • Peters, G. H., S. Toxvaerd, O. H. Olsen, and A. Svendsen. 1996. Dynamics of proteins in different solvent systems: analysis of essential motion in lipases. Biophys. J. 71:2245-2255,.
    • (1996) Biophys. J. , vol.71 , pp. 2245-2255
    • Peters, G.H.1    Toxvaerd, S.2    Olsen, O.H.3    Svendsen, A.4
  • 16
    • 0031042565 scopus 로고    scopus 로고
    • Essential dynamics of lipase binding sites: The effect of inhibitors of different chain length
    • Peters, G. H., D. M. F. van Aalten, A. Svendsen, and R. Bywater. 1997. Essential Dynamics of lipase binding sites: the effect of inhibitors of different chain length. Protein Eng. 10:149-158.
    • (1997) Protein Eng. , vol.10 , pp. 149-158
    • Peters, G.H.1    Van Aalten, D.M.F.2    Svendsen, A.3    Bywater, R.4
  • 17
    • 33646940952 scopus 로고
    • Numerical integration of the Cartesian equations of motion of a system with constraints: Molecular dynamics of n-alkanes
    • Ryckaert, J.-P., G. Ciccotti, and H. J. C. Berendsen. 1977. Numerical integration of the Cartesian equations of motion of a system with constraints: molecular dynamics of n-alkanes. J. Comp. Phys. 23: 327-341.
    • (1977) J. Comp. Phys. , vol.23 , pp. 327-341
    • Ryckaert, J.-P.1    Ciccotti, G.2    Berendsen, H.J.C.3
  • 20
    • 0025005525 scopus 로고
    • Contributions of the large hydrophobic amino acids to the stability of staphylococcal nuclease
    • Shortle, D., W. E. Strites, and A. K. Meeker. 1990. Contributions of the large hydrophobic amino acids to the stability of staphylococcal nuclease. Biochemistry. 29:8033-8041.
    • (1990) Biochemistry , vol.29 , pp. 8033-8041
    • Shortle, D.1    Strites, W.E.2    Meeker, A.K.3
  • 22
    • 0029075795 scopus 로고
    • The essential dynamics of thermolysin-conformation of the hingebending motion and comparison of simulations in vacuum and water
    • van Aalten, D. M. F., A. Amadei, A. B. M. Linssen, V. G. H. Eijsink, and G. Vriend. 1995. The essential dynamics of thermolysin-conformation of the hingebending motion and comparison of simulations in vacuum and water. Proteins Struct. Funct. Genet. 22:45-54.
    • (1995) Proteins Struct. Funct. Genet. , vol.22 , pp. 45-54
    • Van Aalten, D.M.F.1    Amadei, A.2    Linssen, A.B.M.3    Eijsink, V.G.H.4    Vriend, G.5
  • 23
    • 0029586726 scopus 로고    scopus 로고
    • Essential dynamics of the cellular retinol binding protein: Evidence for ligand induced conformational changes
    • van Aalten, D. M. F., J. B. C. Findlay, A. Amadei, and H. J. C. Berendsen. 1996. Essential dynamics of the cellular retinol binding protein: evidence for ligand induced conformational changes. Protein Eng. 8:1129-1135.
    • (1996) Protein Eng. , vol.8 , pp. 1129-1135
    • Van Aalten, D.M.F.1    Findlay, J.B.C.2    Amadei, A.3    Berendsen, H.J.C.4
  • 24
    • 0025398721 scopus 로고
    • WHAT IF: A molecular modeling and drug design program
    • Vriend, G. 1990. WHAT IF: a molecular modeling and drug design program. J. Mol. Graph. 8:52-56.
    • (1990) J. Mol. Graph. , vol.8 , pp. 52-56
    • Vriend, G.1
  • 25
    • 0031893269 scopus 로고    scopus 로고
    • The response of T4 lysozyme to large-to-small substitutions within the core and its relation to the hydrophobic effect
    • Xu, J. A., W. A. Baase, E. Baldwin, and B. W. Matthews. 1998. The response of T4 lysozyme to large-to-small substitutions within the core and its relation to the hydrophobic effect. Protein Sci. 7:158-177.
    • (1998) Protein Sci. , vol.7 , pp. 158-177
    • Xu, J.A.1    Baase, W.A.2    Baldwin, E.3    Matthews, B.W.4
  • 26
    • 0029150760 scopus 로고
    • Protein flexibility and adaptability seen in 25 crystal forms of T4 lysozyme
    • Zhang, X. J., J. A. Wozniak, and B. W. Matthews. 1995. Protein flexibility and adaptability seen in 25 crystal forms of T4 lysozyme. J. Mol. Biol. 250:527-552.
    • (1995) J. Mol. Biol. , vol.250 , pp. 527-552
    • Zhang, X.J.1    Wozniak, J.A.2    Matthews, B.W.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.