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Volumn 48, Issue 2, 2015, Pages 423-430

Keep on moving: Discovering and perturbing the conformational dynamics of enzymes

Author keywords

[No Author keywords available]

Indexed keywords

CYCLOPHILIN A; DIHYDROFOLATE REDUCTASE;

EID: 84923085640     PISSN: 00014842     EISSN: 15204898     Source Type: Journal    
DOI: 10.1021/ar5003158     Document Type: Article
Times cited : (75)

References (73)
  • 1
    • 84861367246 scopus 로고    scopus 로고
    • Biomolecular simulation: A computational microscope for molecular biology
    • Dror, R. O.; Dirks, R. M.; Grossman, J. P.; Xu, H.; Shaw, D. E. Biomolecular simulation: A computational microscope for molecular biology Annu. Rev. Biophys. 2012, 41, 429-452
    • (2012) Annu. Rev. Biophys. , vol.41 , pp. 429-452
    • Dror, R.O.1    Dirks, R.M.2    Grossman, J.P.3    Xu, H.4    Shaw, D.E.5
  • 2
    • 37249032102 scopus 로고    scopus 로고
    • Dynamic personalities of proteins
    • Henzler-Wildman, K.; Kern, D. Dynamic personalities of proteins Nature 2007, 450, 964-972
    • (2007) Nature , vol.450 , pp. 964-972
    • Henzler-Wildman, K.1    Kern, D.2
  • 3
    • 84874181173 scopus 로고    scopus 로고
    • Biochemistry. Integrative structural biology
    • Ward, A. B.; Sali, A.; Wilson, I. A. Biochemistry. Integrative structural biology Science 2013, 339, 913-915
    • (2013) Science , vol.339 , pp. 913-915
    • Ward, A.B.1    Sali, A.2    Wilson, I.A.3
  • 4
    • 84878224305 scopus 로고    scopus 로고
    • Side-chain conformational heterogeneity of intermediates in the Escherichia coli dihydrofolate reductase catalytic cycle
    • Tuttle, L. M.; Dyson, H. J.; Wright, P. E. Side-chain conformational heterogeneity of intermediates in the Escherichia coli dihydrofolate reductase catalytic cycle Biochemistry 2013, 52, 3464-3477
    • (2013) Biochemistry , vol.52 , pp. 3464-3477
    • Tuttle, L.M.1    Dyson, H.J.2    Wright, P.E.3
  • 5
    • 84893419946 scopus 로고    scopus 로고
    • Integrated description of protein dynamics from room-temperature X-ray crystallography and NMR
    • Fenwick, R. B.; van den Bedem, H.; Fraser, J. S.; Wright, P. E. Integrated description of protein dynamics from room-temperature X-ray crystallography and NMR Proc. Natl. Acad. Sci. U.S.A. 2014, 111, E445-454
    • (2014) Proc. Natl. Acad. Sci. U.S.A. , vol.111 , pp. 445-454
    • Fenwick, R.B.1    Van Den Bedem, H.2    Fraser, J.S.3    Wright, P.E.4
  • 6
    • 84883403423 scopus 로고    scopus 로고
    • Automated identification of functional dynamic contact networks from X-ray crystallography
    • van den Bedem, H.; Bhabha, G.; Yang, K.; Wright, P. E.; Fraser, J. S. Automated identification of functional dynamic contact networks from X-ray crystallography Nat. Methods 2013, 10, 896-902
    • (2013) Nat. Methods , vol.10 , pp. 896-902
    • Van Den Bedem, H.1    Bhabha, G.2    Yang, K.3    Wright, P.E.4    Fraser, J.S.5
  • 7
    • 68049085675 scopus 로고    scopus 로고
    • A 21st century revisionist's view at a turning point in enzymology
    • Nagel, Z. D.; Klinman, J. P. A 21st century revisionist's view at a turning point in enzymology Nat. Chem. Biol. 2009, 5, 543-550
    • (2009) Nat. Chem. Biol. , vol.5 , pp. 543-550
    • Nagel, Z.D.1    Klinman, J.P.2
  • 8
    • 77951226274 scopus 로고    scopus 로고
    • At the dawn of the 21st century: Is dynamics the missing link for understanding enzyme catalysis?
    • Kamerlin, S. C.; Warshel, A. At the dawn of the 21st century: Is dynamics the missing link for understanding enzyme catalysis? Proteins 2010, 78, 1339-1375
    • (2010) Proteins , vol.78 , pp. 1339-1375
    • Kamerlin, S.C.1    Warshel, A.2
  • 9
    • 84875685397 scopus 로고    scopus 로고
    • Fundamental challenges in mechanistic enzymology: Progress toward understanding the rate enhancements of enzymes
    • Herschlag, D.; Natarajan, A. Fundamental challenges in mechanistic enzymology: Progress toward understanding the rate enhancements of enzymes Biochemistry 2013, 52, 2050-2067
    • (2013) Biochemistry , vol.52 , pp. 2050-2067
    • Herschlag, D.1    Natarajan, A.2
  • 11
    • 0023847706 scopus 로고
    • Insights into enzyme function from studies on mutants of dihydrofolate reductase
    • Benkovic, S. J.; Fierke, C. A.; Naylor, A. M. Insights into enzyme function from studies on mutants of dihydrofolate reductase Science 1988, 239, 1105-1110
    • (1988) Science , vol.239 , pp. 1105-1110
    • Benkovic, S.J.1    Fierke, C.A.2    Naylor, A.M.3
  • 12
    • 0024569994 scopus 로고
    • Probing the functional role of threonine-113 of Escherichia coli dihydrofolate reductase for its effect on turnover efficiency, catalysis, and binding
    • Fierke, C. A.; Benkovic, S. J. Probing the functional role of threonine-113 of Escherichia coli dihydrofolate reductase for its effect on turnover efficiency, catalysis, and binding Biochemistry 1989, 28, 478-486
    • (1989) Biochemistry , vol.28 , pp. 478-486
    • Fierke, C.A.1    Benkovic, S.J.2
  • 13
    • 0023668190 scopus 로고
    • Construction and evaluation of the kinetic scheme associated with dihydrofolate reductase from Escherichia coli
    • Fierke, C. A.; Johnson, K. A.; Benkovic, S. J. Construction and evaluation of the kinetic scheme associated with dihydrofolate reductase from Escherichia coli Biochemistry 1987, 26, 4085-4092
    • (1987) Biochemistry , vol.26 , pp. 4085-4092
    • Fierke, C.A.1    Johnson, K.A.2    Benkovic, S.J.3
  • 14
    • 0031015737 scopus 로고    scopus 로고
    • Loop and subdomain movements in the mechanism of Escherichia coli dihydrofolate reductase: Crystallographic evidence
    • Sawaya, M. R.; Kraut, J. Loop and subdomain movements in the mechanism of Escherichia coli dihydrofolate reductase: Crystallographic evidence Biochemistry 1997, 36, 586-603
    • (1997) Biochemistry , vol.36 , pp. 586-603
    • Sawaya, M.R.1    Kraut, J.2
  • 15
    • 0026065644 scopus 로고
    • Crystal structure of unliganded Escherichia coli dihydrofolate reductase. Ligand-induced conformational changes and cooperativity in binding
    • Bystroff, C.; Kraut, J. Crystal structure of unliganded Escherichia coli dihydrofolate reductase. Ligand-induced conformational changes and cooperativity in binding Biochemistry 1991, 30, 2227-2239
    • (1991) Biochemistry , vol.30 , pp. 2227-2239
    • Bystroff, C.1    Kraut, J.2
  • 16
    • 0025270551 scopus 로고
    • Crystal structures of Escherichia coli dihydrofolate reductase: The NADP+ holoenzyme and the folate.NADP+ ternary complex. Substrate binding and a model for the transition state
    • Bystroff, C.; Oatley, S. J.; Kraut, J. Crystal structures of Escherichia coli dihydrofolate reductase: The NADP+ holoenzyme and the folate.NADP+ ternary complex. Substrate binding and a model for the transition state Biochemistry 1990, 29, 3263-3277
    • (1990) Biochemistry , vol.29 , pp. 3263-3277
    • Bystroff, C.1    Oatley, S.J.2    Kraut, J.3
  • 17
    • 0028985318 scopus 로고
    • Isomorphous crystal structures of Escherichia coli dihydrofolate reductase complexed with folate, 5-deazafolate, and 5,10-dideazatetrahydrofolate: Mechanistic implications
    • Reyes, V. M.; Sawaya, M. R.; Brown, K. A.; Kraut, J. Isomorphous crystal structures of Escherichia coli dihydrofolate reductase complexed with folate, 5-deazafolate, and 5,10-dideazatetrahydrofolate: Mechanistic implications Biochemistry 1995, 34, 2710-2723
    • (1995) Biochemistry , vol.34 , pp. 2710-2723
    • Reyes, V.M.1    Sawaya, M.R.2    Brown, K.A.3    Kraut, J.4
  • 18
    • 0141746385 scopus 로고    scopus 로고
    • Diagnostic chemical shift markers for loop conformation and substrate and cofactor binding in dihydrofolate reductase complexes
    • Osborne, M. J.; Venkitakrishnan, R. P.; Dyson, H. J.; Wright, P. E. Diagnostic chemical shift markers for loop conformation and substrate and cofactor binding in dihydrofolate reductase complexes Protein Sci. 2003, 12, 2230-2238
    • (2003) Protein Sci. , vol.12 , pp. 2230-2238
    • Osborne, M.J.1    Venkitakrishnan, R.P.2    Dyson, H.J.3    Wright, P.E.4
  • 19
    • 11144328151 scopus 로고    scopus 로고
    • Conformational changes in the active site loops of dihydrofolate reductase during the catalytic cycle
    • Venkitakrishnan, R. P.; Zaborowski, E.; McElheny, D.; Benkovic, S. J.; Dyson, H. J.; Wright, P. E. Conformational changes in the active site loops of dihydrofolate reductase during the catalytic cycle Biochemistry 2004, 43, 16046-16055
    • (2004) Biochemistry , vol.43 , pp. 16046-16055
    • Venkitakrishnan, R.P.1    Zaborowski, E.2    McElheny, D.3    Benkovic, S.J.4    Dyson, H.J.5    Wright, P.E.6
  • 20
    • 33748781457 scopus 로고    scopus 로고
    • The dynamic energy landscape of dihydrofolate reductase catalysis
    • Boehr, D. D.; McElheny, D.; Dyson, H. J.; Wright, P. E. The dynamic energy landscape of dihydrofolate reductase catalysis Science 2006, 313, 1638-1642
    • (2006) Science , vol.313 , pp. 1638-1642
    • Boehr, D.D.1    McElheny, D.2    Dyson, H.J.3    Wright, P.E.4
  • 21
    • 79953823548 scopus 로고    scopus 로고
    • A dynamic knockout reveals that conformational fluctuations influence the chemical step of enzyme catalysis
    • Bhabha, G.; Lee, J.; Ekiert, D. C.; Gam, J.; Wilson, I. A.; Dyson, H. J.; Benkovic, S. J.; Wright, P. E. A dynamic knockout reveals that conformational fluctuations influence the chemical step of enzyme catalysis Science 2011, 332, 234-238
    • (2011) Science , vol.332 , pp. 234-238
    • Bhabha, G.1    Lee, J.2    Ekiert, D.C.3    Gam, J.4    Wilson, I.A.5    Dyson, H.J.6    Benkovic, S.J.7    Wright, P.E.8
  • 24
    • 84890417015 scopus 로고    scopus 로고
    • Preservation of protein dynamics in dihydrofolate reductase evolution
    • Francis, K.; Stojkovic, V.; Kohen, A. Preservation of protein dynamics in dihydrofolate reductase evolution J. Biol. Chem. 2013, 288, 35961-35968
    • (2013) J. Biol. Chem. , vol.288 , pp. 35961-35968
    • Francis, K.1    Stojkovic, V.2    Kohen, A.3
  • 26
    • 0027411746 scopus 로고
    • Effects of point mutation in a flexible loop on the stability and enzymatic function of Escherichia coli dihydrofolate reductase
    • Gekko, K.; Yamagami, K.; Kunori, Y.; Ichihara, S.; Kodama, M.; Iwakura, M. Effects of point mutation in a flexible loop on the stability and enzymatic function of Escherichia coli dihydrofolate reductase J. Biochem. 1993, 113, 74-80
    • (1993) J. Biochem. , vol.113 , pp. 74-80
    • Gekko, K.1    Yamagami, K.2    Kunori, Y.3    Ichihara, S.4    Kodama, M.5    Iwakura, M.6
  • 27
    • 84858121090 scopus 로고    scopus 로고
    • Structure and dynamics of the G121V dihydrofolate reductase mutant: Lessons from a transition-state inhibitor complex
    • Mauldin, R. V.; Sapienza, P. J.; Petit, C. M.; Lee, A. L. Structure and dynamics of the G121V dihydrofolate reductase mutant: lessons from a transition-state inhibitor complex PloS One 2012, 7 e33252
    • (2012) PloS One , vol.7 , pp. 33252
    • Mauldin, R.V.1    Sapienza, P.J.2    Petit, C.M.3    Lee, A.L.4
  • 28
    • 80052149070 scopus 로고    scopus 로고
    • Catalysis by dihydrofolate reductase and other enzymes arises from electrostatic preorganization, not conformational motions
    • Adamczyk, A. J.; Cao, J.; Kamerlin, S. C.; Warshel, A. Catalysis by dihydrofolate reductase and other enzymes arises from electrostatic preorganization, not conformational motions Proc. Natl. Acad. Sci. U.S.A. 2011, 108, 14115-14120
    • (2011) Proc. Natl. Acad. Sci. U.S.A. , vol.108 , pp. 14115-14120
    • Adamczyk, A.J.1    Cao, J.2    Kamerlin, S.C.3    Warshel, A.4
  • 30
    • 84861887134 scopus 로고    scopus 로고
    • Barrier Crossing in Dihydrofolate Reductase does not involve a rate-promoting vibration
    • Dametto, M.; Antoniou, D.; Schwartz, S. D. Barrier Crossing in Dihydrofolate Reductase does not involve a rate-promoting vibration Mol. Phys. 2012, 110, 531-536
    • (2012) Mol. Phys. , vol.110 , pp. 531-536
    • Dametto, M.1    Antoniou, D.2    Schwartz, S.D.3
  • 32
    • 34548660854 scopus 로고    scopus 로고
    • Prolyl cis-trans isomerization as a molecular timer
    • Lu, K. P.; Finn, G.; Lee, T. H.; Nicholson, L. K. Prolyl cis-trans isomerization as a molecular timer Nat. Chem. Biol. 2007, 3, 619-629
    • (2007) Nat. Chem. Biol. , vol.3 , pp. 619-629
    • Lu, K.P.1    Finn, G.2    Lee, T.H.3    Nicholson, L.K.4
  • 33
    • 33746270438 scopus 로고    scopus 로고
    • Cyclophilin, TRIM5, and innate immunity to HIV-1
    • Sokolskaja, E.; Luban, J. Cyclophilin, TRIM5, and innate immunity to HIV-1 Curr. Opin. Microbiol. 2006, 9, 404-408
    • (2006) Curr. Opin. Microbiol. , vol.9 , pp. 404-408
    • Sokolskaja, E.1    Luban, J.2
  • 36
    • 77953977241 scopus 로고    scopus 로고
    • Automated electron-density sampling reveals widespread conformational polymorphism in proteins
    • Lang, P. T.; Ng, H. L.; Fraser, J. S.; Corn, J. E.; Echols, N.; Sales, M.; Holton, J. M.; Alber, T. Automated electron-density sampling reveals widespread conformational polymorphism in proteins Protein Sci. 2010, 19, 1420-1431
    • (2010) Protein Sci. , vol.19 , pp. 1420-1431
    • Lang, P.T.1    Ng, H.L.2    Fraser, J.S.3    Corn, J.E.4    Echols, N.5    Sales, M.6    Holton, J.M.7    Alber, T.8
  • 37
    • 84872151410 scopus 로고    scopus 로고
    • Conformational plasticity of an enzyme during catalysis: Intricate coupling between cyclophilin A dynamics and substrate turnover
    • McGowan, L. C.; Hamelberg, D. Conformational plasticity of an enzyme during catalysis: Intricate coupling between cyclophilin A dynamics and substrate turnover Biophys. J. 2013, 104, 216-226
    • (2013) Biophys. J. , vol.104 , pp. 216-226
    • McGowan, L.C.1    Hamelberg, D.2
  • 40
    • 0035807809 scopus 로고    scopus 로고
    • Enzyme-like proteins by computational design
    • Bolon, D. N.; Mayo, S. L. Enzyme-like proteins by computational design Proc. Natl. Acad. Sci. U.S.A. 2001, 98, 14274-14279
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , pp. 14274-14279
    • Bolon, D.N.1    Mayo, S.L.2
  • 43
    • 77649271939 scopus 로고    scopus 로고
    • Evolutionary optimization of computationally designed enzymes: Kemp eliminases of the KE07 series
    • Khersonsky, O.; Rothlisberger, D.; Dym, O.; Albeck, S.; Jackson, C. J.; Baker, D.; Tawfik, D. S. Evolutionary optimization of computationally designed enzymes: Kemp eliminases of the KE07 series J. Mol. Biol. 2010, 396, 1025-1042
    • (2010) J. Mol. Biol. , vol.396 , pp. 1025-1042
    • Khersonsky, O.1    Rothlisberger, D.2    Dym, O.3    Albeck, S.4    Jackson, C.J.5    Baker, D.6    Tawfik, D.S.7
  • 45
    • 84863000087 scopus 로고    scopus 로고
    • Bridging the gaps in design methodologies by evolutionary optimization of the stability and proficiency of designed Kemp eliminase KE59
    • Khersonsky, O.; Kiss, G.; Rothlisberger, D.; Dym, O.; Albeck, S.; Houk, K. N.; Baker, D.; Tawfik, D. S. Bridging the gaps in design methodologies by evolutionary optimization of the stability and proficiency of designed Kemp eliminase KE59 Proc. Natl. Acad. Sci. U.S.A. 2012, 109, 10358-10363
    • (2012) Proc. Natl. Acad. Sci. U.S.A. , vol.109 , pp. 10358-10363
    • Khersonsky, O.1    Kiss, G.2    Rothlisberger, D.3    Dym, O.4    Albeck, S.5    Houk, K.N.6    Baker, D.7    Tawfik, D.S.8
  • 46
    • 77950437360 scopus 로고    scopus 로고
    • Origins of catalysis by computationally designed retroaldolase enzymes
    • Lassila, J. K.; Baker, D.; Herschlag, D. Origins of catalysis by computationally designed retroaldolase enzymes Proc. Natl. Acad. Sci. U.S.A. 2010, 107, 4937-4942
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , pp. 4937-4942
    • Lassila, J.K.1    Baker, D.2    Herschlag, D.3
  • 47
    • 84888094913 scopus 로고    scopus 로고
    • The effect of the hydrophobic environment on the retro-aldol reaction: Comparison to a computationally-designed enzyme
    • Schmidt, J.; Ehasz, C.; Epperson, M.; Klas, K.; Wyatt, J.; Hennig, M.; Forconi, M. The effect of the hydrophobic environment on the retro-aldol reaction: comparison to a computationally-designed enzyme Org. Biomol. Chem. 2013, 11, 8419-8425
    • (2013) Org. Biomol. Chem. , vol.11 , pp. 8419-8425
    • Schmidt, J.1    Ehasz, C.2    Epperson, M.3    Klas, K.4    Wyatt, J.5    Hennig, M.6    Forconi, M.7
  • 48
    • 84880920662 scopus 로고    scopus 로고
    • Evolution of a designed retro-aldolase leads to complete active site remodeling
    • Giger, L.; Caner, S.; Obexer, R.; Kast, P.; Baker, D.; Ban, N.; Hilvert, D. Evolution of a designed retro-aldolase leads to complete active site remodeling Nat. Chem. Biol. 2013, 9, 494-498
    • (2013) Nat. Chem. Biol. , vol.9 , pp. 494-498
    • Giger, L.1    Caner, S.2    Obexer, R.3    Kast, P.4    Baker, D.5    Ban, N.6    Hilvert, D.7
  • 51
    • 84874023884 scopus 로고    scopus 로고
    • Molecular dynamics simulations for the ranking, evaluation, and refinement of computationally designed proteins
    • Kiss, G.; Pande, V. S.; Houk, K. N. Molecular dynamics simulations for the ranking, evaluation, and refinement of computationally designed proteins Methods Enzymol. 2013, 523, 145-170
    • (2013) Methods Enzymol. , vol.523 , pp. 145-170
    • Kiss, G.1    Pande, V.S.2    Houk, K.N.3
  • 53
    • 64849101493 scopus 로고    scopus 로고
    • Protein dynamism and evolvability
    • Tokuriki, N.; Tawfik, D. S. Protein dynamism and evolvability Science 2009, 324, 203-207
    • (2009) Science , vol.324 , pp. 203-207
    • Tokuriki, N.1    Tawfik, D.S.2
  • 54
    • 84904466057 scopus 로고    scopus 로고
    • Catalytic efficiency of designed catalytic proteins
    • Korendovych, I. V.; DeGrado, W. F. Catalytic efficiency of designed catalytic proteins Curr. Opin. Struct. Biol. 2014, 27C, 113-121
    • (2014) Curr. Opin. Struct. Biol. , vol.27 , pp. 113-121
    • Korendovych, I.V.1    Degrado, W.F.2
  • 55
    • 70349632843 scopus 로고    scopus 로고
    • The influence of protein dynamics on the success of computational enzyme design
    • Ruscio, J. Z.; Kohn, J. E.; Ball, K. A.; Head-Gordon, T. The influence of protein dynamics on the success of computational enzyme design J. Am. Chem. Soc. 2009, 131, 14111-14115
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 14111-14115
    • Ruscio, J.Z.1    Kohn, J.E.2    Ball, K.A.3    Head-Gordon, T.4
  • 58
    • 84880848354 scopus 로고    scopus 로고
    • Electron counting and beam-induced motion correction enable near-atomic-resolution single-particle cryo-EM
    • Li, X.; Mooney, P.; Zheng, S.; Booth, C. R.; Braunfeld, M. B.; Gubbens, S.; Agard, D. A.; Cheng, Y. Electron counting and beam-induced motion correction enable near-atomic-resolution single-particle cryo-EM Nat. Methods 2013, 10, 584-590
    • (2013) Nat. Methods , vol.10 , pp. 584-590
    • Li, X.1    Mooney, P.2    Zheng, S.3    Booth, C.R.4    Braunfeld, M.B.5    Gubbens, S.6    Agard, D.A.7    Cheng, Y.8
  • 59
    • 84855818650 scopus 로고    scopus 로고
    • A Bayesian view on cryo-EM structure determination
    • Scheres, S. H. A Bayesian view on cryo-EM structure determination J. Mol. Biol. 2012, 415, 406-418
    • (2012) J. Mol. Biol. , vol.415 , pp. 406-418
    • Scheres, S.H.1
  • 60
    • 33645834303 scopus 로고    scopus 로고
    • New tools provide new insights in NMR studies of protein dynamics
    • Mittermaier, A.; Kay, L. E. New tools provide new insights in NMR studies of protein dynamics Science 2006, 312, 224-228
    • (2006) Science , vol.312 , pp. 224-228
    • Mittermaier, A.1    Kay, L.E.2
  • 62
    • 34447503697 scopus 로고    scopus 로고
    • Conformational entropy in molecular recognition by proteins
    • Frederick, K. K.; Marlow, M. S.; Valentine, K. G.; Wand, A. J. Conformational entropy in molecular recognition by proteins Nature 2007, 448, 325-329
    • (2007) Nature , vol.448 , pp. 325-329
    • Frederick, K.K.1    Marlow, M.S.2    Valentine, K.G.3    Wand, A.J.4
  • 63
    • 0020648847 scopus 로고
    • The role of mobility in the substrate binding and catalytic machinery of enzymes
    • Alber, T.; Gilbert, W. A.; Ponzi, D. R.; Petsko, G. A. The role of mobility in the substrate binding and catalytic machinery of enzymes Ciba Found. Symp. 1983, 93, 4-24
    • (1983) Ciba Found. Symp. , vol.93 , pp. 4-24
    • Alber, T.1    Gilbert, W.A.2    Ponzi, D.R.3    Petsko, G.A.4
  • 65
    • 69549120472 scopus 로고    scopus 로고
    • Conformational selection or induced fit: A flux description of reaction mechanism
    • Hammes, G. G.; Chang, Y. C.; Oas, T. G. Conformational selection or induced fit: a flux description of reaction mechanism Proc. Natl. Acad. Sci. U.S.A. 2009, 106, 13737-13741
    • (2009) Proc. Natl. Acad. Sci. U.S.A. , vol.106 , pp. 13737-13741
    • Hammes, G.G.1    Chang, Y.C.2    Oas, T.G.3
  • 66
    • 84864462749 scopus 로고    scopus 로고
    • Conformational selection or induced fit? A critical appraisal of the kinetic mechanism
    • Vogt, A. D.; Di Cera, E. Conformational selection or induced fit? A critical appraisal of the kinetic mechanism Biochemistry 2012, 51, 5894-5902
    • (2012) Biochemistry , vol.51 , pp. 5894-5902
    • Vogt, A.D.1    Di Cera, E.2
  • 67
    • 84903133311 scopus 로고    scopus 로고
    • Incorporation of protein flexibility and conformational energy penalties in docking screens to improve ligand discovery
    • Fischer, M.; Coleman, R. G.; Fraser, J. S.; Shoichet, B. K. Incorporation of protein flexibility and conformational energy penalties in docking screens to improve ligand discovery Nat. Chem. 2014, 6, 575-583
    • (2014) Nat. Chem. , vol.6 , pp. 575-583
    • Fischer, M.1    Coleman, R.G.2    Fraser, J.S.3    Shoichet, B.K.4
  • 68
    • 50849111095 scopus 로고    scopus 로고
    • Conformational relaxation following hydride transfer plays a limiting role in dihydrofolate reductase catalysis
    • Boehr, D. D.; Dyson, H. J.; Wright, P. E. Conformational relaxation following hydride transfer plays a limiting role in dihydrofolate reductase catalysis Biochemistry 2008, 47, 9227-9233
    • (2008) Biochemistry , vol.47 , pp. 9227-9233
    • Boehr, D.D.1    Dyson, H.J.2    Wright, P.E.3
  • 69
    • 84882746143 scopus 로고    scopus 로고
    • Conformational motions regulate phosphoryl transfer in related protein tyrosine phosphatases
    • Whittier, S. K.; Hengge, A. C.; Loria, J. P. Conformational motions regulate phosphoryl transfer in related protein tyrosine phosphatases Science 2013, 341, 899-903
    • (2013) Science , vol.341 , pp. 899-903
    • Whittier, S.K.1    Hengge, A.C.2    Loria, J.P.3
  • 70
    • 84898821640 scopus 로고    scopus 로고
    • Understanding the mechanism of proteasome 20S core particle gating
    • Latham, M. P.; Sekhar, A.; Kay, L. E. Understanding the mechanism of proteasome 20S core particle gating Proc. Natl. Acad. Sci. U.S.A. 2014, 111, 5532-5537
    • (2014) Proc. Natl. Acad. Sci. U.S.A. , vol.111 , pp. 5532-5537
    • Latham, M.P.1    Sekhar, A.2    Kay, L.E.3
  • 71
    • 48249095613 scopus 로고    scopus 로고
    • Single-molecule approach to molecular biology in living bacterial cells
    • Xie, X. S.; Choi, P. J.; Li, G. W.; Lee, N. K.; Lia, G. Single-molecule approach to molecular biology in living bacterial cells Annu. Rev. Biophys. 2008, 37, 417-444
    • (2008) Annu. Rev. Biophys. , vol.37 , pp. 417-444
    • Xie, X.S.1    Choi, P.J.2    Li, G.W.3    Lee, N.K.4    Lia, G.5
  • 73
    • 84862225325 scopus 로고    scopus 로고
    • Functional modulation of a protein folding landscape via side-chain distortion
    • Kelch, B. A.; Salimi, N. L.; Agard, D. A. Functional modulation of a protein folding landscape via side-chain distortion Proc. Natl. Acad. Sci. U.S.A. 2012, 109, 9414-9419
    • (2012) Proc. Natl. Acad. Sci. U.S.A. , vol.109 , pp. 9414-9419
    • Kelch, B.A.1    Salimi, N.L.2    Agard, D.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.