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Volumn 113, Issue 8, 2009, Pages 2225-2230

Fluctuating enzyme and its biological functions: Positive cooperativity without multiple states

Author keywords

[No Author keywords available]

Indexed keywords

CATALYSTS; DRUG INTERACTIONS;

EID: 65249133487     PISSN: 15206106     EISSN: None     Source Type: Journal    
DOI: 10.1021/jp810657j     Document Type: Article
Times cited : (20)

References (53)
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    • Herve, G, Ed, CRC Press: Boca Raton, FL
    • (c) Ricard, J. In Allosteric Enzymes; Herve', G., Ed.; CRC Press: Boca Raton, FL, 1989; pp 1-25.
    • (1989) Allosteric Enzymes , pp. 1-25
    • Ricard, J.1
  • 14
    • 46749083416 scopus 로고    scopus 로고
    • Qian, H Biophys. J. 2008, 95, 10-17.
    • (2008) Biophys. J , vol.95 , pp. 10-17
    • Qian, H.1
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    • 33748096830 scopus 로고    scopus 로고
    • (b) Qian, H. J. Phys. Chem. B 2006, 110, 15063-15074.
    • (2006) J. Phys. Chem. B , vol.110 , pp. 15063-15074
    • Qian, H.1
  • 21
    • 0004043557 scopus 로고
    • Welch, G. R, Ed, John Wiley & Sons: New York
    • (a) The Fluctuating Enzyme; Welch, G. R., Ed.; John Wiley & Sons: New York, 1986.
    • (1986) The Fluctuating Enzyme
  • 26
    • 84906362860 scopus 로고    scopus 로고
    • Conformational changes, well studied at the time scale of milliseconds due to ligand bindings and/or chemical modifications, and conformational dynamics, as demonstrated by amide proton hydrogen exchange and molecular dynamic calculations occurring on the picosecond time scale, are often lumped together in most biochemical discussions. A more precise distinction perhaps can be made in terms of the single versus multiple states. For more discussion, see:
    • Conformational changes, well studied at the time scale of milliseconds due to ligand bindings and/or chemical modifications, and conformational dynamics, as demonstrated by amide proton hydrogen exchange and molecular dynamic calculations occurring on the picosecond time scale, are often lumped together in most biochemical discussions. A more precise distinction perhaps can be made in terms of the single versus multiple states. For more discussion, see:
  • 28
    • 0031582071 scopus 로고    scopus 로고
    • (b) Qian, H. J. Mol. Biol. 1997, 267, 198-206.
    • (1997) J. Mol. Biol , vol.267 , pp. 198-206
    • Qian, H.1
  • 30
    • 84906377093 scopus 로고    scopus 로고
    • In allosteric cooperativity, one of the differences between the Monod-Wyman-Changeux model and the Koshland-Nemethy-Filmer model is that the former has a two-state transition in response to ligand concentration while the latter has a single-state transition, see ref 1. In the MWC model, the T and R states always co-exist, irrespective of the ligand concentration. The ligand binding shifts the relative energy, and thus the relative population, between the T and R. In contrast, the KNF model has a gradual (in four steps) change of the tetramer structure with increasing ligand binding. There is a tighter coupling between the binding and the subunit structure in the KNF model
    • In allosteric cooperativity, one of the differences between the Monod-Wyman-Changeux model and the Koshland-Nemethy-Filmer model is that the former has a "two-state" transition in response to ligand concentration while the latter has a single-state transition, see ref 1. In the MWC model, the T and R states always co-exist, irrespective of the ligand concentration. The ligand binding shifts the relative energy, and thus the relative population, between the T and R. In contrast, the KNF model has a "gradual" (in four steps) change of the tetramer structure with increasing ligand binding. There is a tighter coupling between the binding and the subunit structure in the KNF model.
  • 33
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    • Welch, G. R, Ed, John Wiley: New York
    • Volkenstein, M. V. In Fluctuating Enzyme; Welch, G. R., Ed.; John Wiley: New York, 1986; pp 403-419.
    • (1986) Fluctuating Enzyme , pp. 403-419
    • Volkenstein, M.V.1
  • 52
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    • Phase diagram characterization of complex kinetics of fluctuating enzymes: Lessons from a minimal model
    • Manuscript in preparation
    • (a) Min, W.; Jiang, L.; Xie, X. S. Phase diagram characterization of complex kinetics of fluctuating enzymes: Lessons from a minimal model. Manuscript in preparation.
    • Min, W.1    Jiang, L.2    Xie, X.S.3
  • 53
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    • Enzyme kinetics as a non-equilibrium steady-state cycle on a two-dimensional reaction free energy surface
    • Manuscript in preparation
    • (b) Min, W.; Xie, X. S.; Bagchi, B. Enzyme kinetics as a non-equilibrium steady-state cycle on a two-dimensional reaction free energy surface. Manuscript in preparation.
    • Min, W.1    Xie, X.S.2    Bagchi, B.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.