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Volumn 10, Issue 2, 2009, Pages 110-115

Allosteric coupling and conformational fluctuations in proteins

Author keywords

Allosteric coupling; Conformational fluctuation; COREX algorithm; Native ensemble; Protein function; Protein substates

Indexed keywords

ALGORITHM; ALLOSTERISM; LIGAND BINDING; MATHEMATICAL COMPUTING; MATHEMATICAL MODEL; PROBABILITY; PROTEIN CONFORMATION; PROTEIN FUNCTION; PROTEIN PROTEIN INTERACTION; PROTEIN STRUCTURE; QUANTITATIVE ANALYSIS; REGULATORY MECHANISM; REVIEW; STRUCTURE ACTIVITY RELATION; THERMODYNAMICS;

EID: 65649102991     PISSN: 13892037     EISSN: None     Source Type: Journal    
DOI: 10.2174/138920309787847644     Document Type: Review
Times cited : (18)

References (23)
  • 1
    • 78651189765 scopus 로고    scopus 로고
    • Monod, J., Wyman, J., and Changeux, J.P. On the nature of allosteric transitions: A plausible model. (1965) J. Mol. Biol., 12, 88-118.
    • Monod, J., Wyman, J., and Changeux, J.P. On the nature of allosteric transitions: A plausible model. (1965) J. Mol. Biol., 12, 88-118.
  • 2
    • 20344370764 scopus 로고    scopus 로고
    • Changeux, J.P. and Edelstein, S.J. Allosteric mechanisms of signal transduction (2005) Science, 308, 1424-1428.
    • Changeux, J.P. and Edelstein, S.J. Allosteric mechanisms of signal transduction (2005) Science, 308, 1424-1428.
  • 3
    • 0037133221 scopus 로고    scopus 로고
    • Frauenfelder, H. Proteins: paradigms of complexity. (2002) Proc. Natl. Acad. Sci. USA, 99, 2479-2480.
    • Frauenfelder, H. Proteins: paradigms of complexity. (2002) Proc. Natl. Acad. Sci. USA, 99, 2479-2480.
  • 4
    • 0004244695 scopus 로고
    • Mill Valley, California University Science Books
    • Wyman, J. and Gill, S.J. (1990) Binding and Linkage. Mill Valley, California University Science Books.
    • (1990) Binding and Linkage
    • Wyman, J.1    Gill, S.J.2
  • 5
    • 0003918423 scopus 로고
    • Chapman and Hall, New York, London
    • Weber, G. (1992) Protein interactions. Chapman and Hall, New York, London.
    • (1992) Protein interactions
    • Weber, G.1
  • 6
    • 0025126043 scopus 로고    scopus 로고
    • Horovitz, A. and Fersht, A.R. Strategy for analysing the cooperativity of intramolecular interactions in peptides and proteins. (1990) J. Mol. Biol., 214, 613-617.
    • Horovitz, A. and Fersht, A.R. Strategy for analysing the cooperativity of intramolecular interactions in peptides and proteins. (1990) J. Mol. Biol., 214, 613-617.
  • 7
    • 0000164734 scopus 로고    scopus 로고
    • Di Cera, E. Site-Specific Thermodynamics: Understanding Cooperativity in Molecular Recognition. (1998) Chem. Rev., 98, 1563-1591.
    • Di Cera, E. Site-Specific Thermodynamics: Understanding Cooperativity in Molecular Recognition. (1998) Chem. Rev., 98, 1563-1591.
  • 8
    • 0023041574 scopus 로고    scopus 로고
    • Zimmerberg, J. and Parsegian, V.A. Polymer inaccessible changes during opening and closing of a voltage-dependent ionic channel. ( 1986) Nature, 323, 36-39.
    • Zimmerberg, J. and Parsegian, V.A. Polymer inaccessible volume changes during opening and closing of a voltage-dependent ionic channel. ( 1986) Nature, 323, 36-39.
  • 9
    • 0016828929 scopus 로고    scopus 로고
    • Austin, R.H., Beeson, K.W., Eisenstein, L., Frauenfelder, H. and Gunsalus I. C. Dynamics of ligand binding to myoglobin. (1975) Biochemistry, 14, 1541-5373.
    • Austin, R.H., Beeson, K.W., Eisenstein, L., Frauenfelder, H. and Gunsalus I. C. Dynamics of ligand binding to myoglobin. (1975) Biochemistry, 14, 1541-5373.
  • 10
    • 0023746244 scopus 로고    scopus 로고
    • Frauenfelder, H., Parak, F. and Young, R.D. Conformational substates in proteins. (1988) Ann. Rev. Biophys. Biophys. Chem., 17, 451-479.
    • Frauenfelder, H., Parak, F. and Young, R.D. Conformational substates in proteins. (1988) Ann. Rev. Biophys. Biophys. Chem., 17, 451-479.
  • 11
    • 0000229165 scopus 로고    scopus 로고
    • Šrajer, V.V., Schomacker, K.T. and Champion P.M. Spectral broadening in biomolecules. (1986) Phys. Rev. Lett. 57, 1267-1270.
    • Šrajer, V.V., Schomacker, K.T. and Champion P.M. Spectral broadening in biomolecules. (1986) Phys. Rev. Lett. 57, 1267-1270.
  • 12
    • 0023357309 scopus 로고    scopus 로고
    • Alcala, J.R., Gratton, E. and Prendergast, F.G. Interpretation of fluorescence decays in proteins using continuous lifetime distributions. (1987) Biophys. J., 51, 925-936.
    • Alcala, J.R., Gratton, E. and Prendergast, F.G. Interpretation of fluorescence decays in proteins using continuous lifetime distributions. (1987) Biophys. J., 51, 925-936.
  • 13
    • 0001000772 scopus 로고    scopus 로고
    • Yang, I.-S. and Anderson, A.C. Specific heat of melanin at temperatures below 3 K. (1986) Phys. Rev. B, 34, 2942-2944.
    • Yang, I.-S. and Anderson, A.C. Specific heat of melanin at temperatures below 3 K. (1986) Phys. Rev. B, 34, 2942-2944.
  • 14
    • 34250142589 scopus 로고    scopus 로고
    • Singh G.P., Schink H.J., Löhneysen, H., Parak, F. and Hunklinger, S. Excitations in Metmyoglobin crystals at low temperatures (1984) Z. Phys., 55, 23-26.
    • Singh G.P., Schink H.J., Löhneysen, H., Parak, F. and Hunklinger, S. Excitations in Metmyoglobin crystals at low temperatures (1984) Z. Phys., 55, 23-26.
  • 15
    • 5144223810 scopus 로고    scopus 로고
    • Fenimore, P.W., Frauenfelder, H., McMahon, B.H. and Young, R.D. Bulk-solvent and hydration-shell fluctuations, similar to alpha- and beta-fluctuations in glasses, control protein motions and functions. ( 2004) Proc. Natl. Acad. Sci. USA, 101, 14408-14413.
    • Fenimore, P.W., Frauenfelder, H., McMahon, B.H. and Young, R.D. Bulk-solvent and hydration-shell fluctuations, similar to alpha- and beta-fluctuations in glasses, control protein motions and functions. ( 2004) Proc. Natl. Acad. Sci. USA, 101, 14408-14413.
  • 16
    • 0001870572 scopus 로고    scopus 로고
    • Onaran, H.O. and Costa, T. Agonist efficacy and allosteric models of receptor action. (1997) Ann. N.Y. Acad. Sci. 812, 98-115.
    • Onaran, H.O. and Costa, T. Agonist efficacy and allosteric models of receptor action. (1997) Ann. N.Y. Acad. Sci. 812, 98-115.
  • 19
    • 0022114079 scopus 로고    scopus 로고
    • Ansari, A., Berendzen, J., Bowne, S.F., Frauenfelder, H., Iben, I.E., Sauke, T.B., Shyamsunder, E., and Young, R.D. Protein states and proteinquakes. (1985) Proc. Natl. Acad. Sci. USA, 82, 5000-5004.
    • Ansari, A., Berendzen, J., Bowne, S.F., Frauenfelder, H., Iben, I.E., Sauke, T.B., Shyamsunder, E., and Young, R.D. Protein states and proteinquakes. (1985) Proc. Natl. Acad. Sci. USA, 82, 5000-5004.
  • 20
    • 0030580089 scopus 로고    scopus 로고
    • Hilser, V.J. and Freire, E. Structure-based calculation of the equilibrium folding pathway of proteins. Correlation with hydrogen exchange protection factors. (1996) J. Mol. Biol. 262, 756-772.
    • Hilser, V.J. and Freire, E. Structure-based calculation of the equilibrium folding pathway of proteins. Correlation with hydrogen exchange protection factors. (1996) J. Mol. Biol. 262, 756-772.
  • 21
    • 0031042186 scopus 로고    scopus 로고
    • Hilser, V.J. and Freire, E. Predicting the equilibrium protein folding pathway: structure-based analysis of staphylococcal nuclease. (1997) Protein Struct. Funct. Genet. 27, 171-183.
    • Hilser, V.J. and Freire, E. Predicting the equilibrium protein folding pathway: structure-based analysis of staphylococcal nuclease. (1997) Protein Struct. Funct. Genet. 27, 171-183.
  • 22
    • 0032544060 scopus 로고    scopus 로고
    • Hilser, V.J., Dowdy, D., Oas, T.G. and Freire, E. The structural distribution of cooperative interactions in proteins: analysis of the native state ensemble. (1998) Proc. Natl. Acad. Sci. USA, 95, 9903-9908.
    • Hilser, V.J., Dowdy, D., Oas, T.G. and Freire, E. The structural distribution of cooperative interactions in proteins: analysis of the native state ensemble. (1998) Proc. Natl. Acad. Sci. USA, 95, 9903-9908.
  • 23
    • 33646922285 scopus 로고    scopus 로고
    • Hilser, V.J., Garcia-Moreno, E.B., Oas, T.G., Kapp, G. and Whitten, S.T. A statistical thermodynamic model of the protein ensemble. (2006) Chem. Rev. 106, 1545-1558.
    • Hilser, V.J., Garcia-Moreno, E.B., Oas, T.G., Kapp, G. and Whitten, S.T. A statistical thermodynamic model of the protein ensemble. (2006) Chem. Rev. 106, 1545-1558.


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.