메뉴 건너뛰기




Volumn 2, Issue 2, 2008, Pages 61-64

Energy landscape along an enzymatic reaction trajectory: Hinges or cracks?

Author keywords

[No Author keywords available]

Indexed keywords


EID: 61949448788     PISSN: 19552068     EISSN: 1955205X     Source Type: Journal    
DOI: 10.2976/1.2894846     Document Type: Article
Times cited : (56)

References (26)
  • 1
    • 36749008588 scopus 로고    scopus 로고
    • Large-scale allosteric conformational transitions of adenylate kinase appear to involve a population shift mechanism
    • Arora, K, and Brooks, CL, III (2007). "Large-scale allosteric conformational transitions of adenylate kinase appear to involve a population shift mechanism." Proc. Natl. Acad. Sci. U.S.A. 104, 18496-18501.
    • (2007) Proc. Natl. Acad. Sci. U.S.A , vol.104 , pp. 18496-18501
    • Arora, K.1    Brooks III, C.L.2
  • 3
    • 0023449962 scopus 로고
    • Spin glasses and the statisticalmechanics of protein folding
    • Bryngelson, JD, and Wolynes, PG (1987). "Spin glasses and the statisticalmechanics of protein folding." Proc. Natl. Acad. Sci. U.S.A. 84, 7524-7528.
    • (1987) Proc. Natl. Acad. Sci. U.S.A , vol.84 , pp. 7524-7528
    • Bryngelson, J.D.1    Wolynes, P.G.2
  • 4
    • 0029086917 scopus 로고
    • Activation of chicken liver dihydrofolate-reductase in concentrated urea solutions
    • Fan, YX, Ju, M, Zhou, JM, and Tsou, CL (1995). "Activation of chicken liver dihydrofolate-reductase in concentrated urea solutions." Biochim. Biophys. Acta 1252, 151-157.
    • (1995) Biochim. Biophys. Acta , vol.1252 , pp. 151-157
    • Fan, Y.X.1    Ju, M.2    Zhou, J.M.3    Tsou, C.L.4
  • 7
    • 0026320866 scopus 로고
    • The energy landscapes of motions of proteins
    • Frauenfelder, H, Sligar, SG, and Wolynes, PG (1991). "The energy landscapes of motions of proteins." Science 254, 1598-1603.
    • (1991) Science , vol.254 , pp. 1598-1603
    • Frauenfelder, H.1    Sligar, S.G.2    Wolynes, P.G.3
  • 8
    • 0004214524 scopus 로고
    • Longmans Green, NewYork, NY
    • Haldane, JBS (1930). Enzymes, Longmans Green, NewYork, NY.
    • (1930) Enzymes
    • Haldane, J.B.S.1
  • 11
    • 33847770916 scopus 로고    scopus 로고
    • Internal strain regulates the nucleotide binding site of the kinesin leading head
    • Hyeon, C, and Onuchic, JN (2007a). "Internal strain regulates the nucleotide binding site of the kinesin leading head." Proc. Natl. Acad. Sci. U.S.A. 104, 2175-2180.
    • (2007) Proc. Natl. Acad. Sci. U.S.A. , vol.104 , pp. 2175-2180
    • Hyeon, C.1    Onuchic, J.N.2
  • 12
    • 36849010909 scopus 로고    scopus 로고
    • Mechanical control of the directional stepping dynamics of the kinesin motor
    • Hyeon, C, and Onuchic, JN (2007b). "Mechanical control of the directional stepping dynamics of the kinesin motor." Proc. Natl. Acad. Sci. U.S.A. 104, 17382-17387.
    • (2007) Proc. Natl. Acad. Sci. U.S.A. , vol.104 , pp. 17382-17387
    • Hyeon, C.1    Onuchic, J.N.2
  • 13
    • 0026723063 scopus 로고
    • Protein folding funnels-A kinetic approach to the sequence structure relationship
    • Leopold, PE, Montal, M, and Onuchic, JN (1992). "Protein folding funnels-A kinetic approach to the sequence structure relationship." Proc. Natl. Acad. Sci. U.S.A. 89, 8721-8725.
    • (1992) Proc. Natl. Acad. Sci. U.S.A. , vol.89 , pp. 8721-8725
    • Leopold, P.E.1    Montal, M.2    Onuchic, J.N.3
  • 15
    • 0242268469 scopus 로고    scopus 로고
    • Nonlinear elasticity, proteinquakes, and the energy landscapes of functional transitions in proteins
    • Miyashita, O, Onuchic, JN, and Wolynes, PG (2003). "Nonlinear elasticity, proteinquakes, and the energy landscapes of functional transitions in proteins." Proc. Natl. Acad. Sci. U.S.A. 100, 12570-12575.
    • (2003) Proc. Natl. Acad. Sci. U.S.A. , vol.100 , pp. 12570-12575
    • Miyashita, O.1    Onuchic, J.N.2    Wolynes, P.G.3
  • 17
    • 0000421878 scopus 로고
    • Nature of forces between large molecules of biological interest
    • Pauling, L (1948). "Nature of forces between large molecules of biological interest." Nature (London) 161, 707-709.
    • (1948) Nature (London) , vol.161 , pp. 707-709
    • Pauling, L.1
  • 18
    • 0036307741 scopus 로고    scopus 로고
    • The mechanism and pathway of pH induced swelling in cowpea chlorotic mottle virus
    • Tama, F, and Brooks, CL, III (2002). "The mechanism and pathway of pH induced swelling in cowpea chlorotic mottle virus." J. Mol. Biol. 318, 733-747.
    • (2002) J. Mol. Biol. , vol.318 , pp. 733-747
    • Tama, F.1    Brooks III, C.L.2
  • 19
    • 0035044995 scopus 로고    scopus 로고
    • Conformational change of proteins arising from normal mode calculations
    • Tama, F, and Sanjouand, YH (2001). "Conformational change of proteins arising from normal mode calculations." Protein Eng. 14, 1-6.
    • (2001) Protein Eng , vol.14 , pp. 1-6
    • Tama, F.1    Sanjouand, Y.H.2
  • 20
    • 0000197372 scopus 로고    scopus 로고
    • Large amplitude motions in proteins from a singleparameter, atomic analysis
    • Tiron, MM (1996). "Large amplitude motions in proteins from a singleparameter, atomic analysis." Phys. Rev. Lett. 77, 1905-1908.
    • (1996) Phys. Rev. Lett. , vol.77 , pp. 1905-1908
    • Tiron, M.M.1
  • 21
    • 0016412390 scopus 로고
    • Energetics of ligand binding to proteins
    • Weber, G (1975). "Energetics of ligand binding to proteins." Adv. Protein Chem. 29, 1-83.
    • (1975) Adv. Protein Chem. , vol.29 , pp. 1-83
    • Weber, G.1
  • 22
    • 33846847773 scopus 로고    scopus 로고
    • Conformational transitions of adenylate kinase: Switching by cracking
    • Whitford, PC, Miyashita, O, Levy, Y, and Onuchic, JN (2007). "Conformational transitions of adenylate kinase: switching by cracking." J. Mol. Biol. 366, 1661-1667.
    • (2007) J. Mol. Biol. , vol.366 , pp. 1661-1667
    • Whitford, P.C.1    Miyashita, O.2    Levy, Y.3    Onuchic, J.N.4
  • 23
    • 38349092279 scopus 로고    scopus 로고
    • Conformational transitions in adenylate kinase: Allosteric communication reduces misligation
    • Whitford, PC, Gosavi, S, and Onuchic, JN (2008). "Conformational transitions in adenylate kinase: allosteric communication reduces misligation." J. Biol. Chem. 283, 2042-2048.
    • (2008) J. Biol. Chem. , vol.283 , pp. 2042-2048
    • Whitford, P.C.1    Gosavi, S.2    Onuchic, J.N.3
  • 25
    • 37548999364 scopus 로고    scopus 로고
    • Force generation in kinesin hinges on cover-neck bundle formation
    • Wonmuk, H, Lang, MJ, and Karplus, M (2008). "Force generation in kinesin hinges on cover-neck bundle formation." Structure (London) 16, 62-71.
    • (2008) Structure (London) , vol.16 , pp. 62-71
    • Wonmuk, H.1    Lang, M.J.2    Karplus, M.3
  • 26
    • 0031577566 scopus 로고    scopus 로고
    • Activation of adenylate kinase by denaturants is due to the increasing conformational flexibility at its active sites
    • Zhang, HJ, Sheng, XR, Pan, XM, and Zhou, JM (1997). "Activation of adenylate kinase by denaturants is due to the increasing conformational flexibility at its active sites." Biochem. Biophys. Res. Commun. 238, 382-386.
    • (1997) Biochem. Biophys. Res. Commun. , vol.238 , pp. 382-386
    • Zhang, H.J.1    Sheng, X.R.2    Pan, X.M.3    Zhou, J.M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.