메뉴 건너뛰기




Volumn 43, Issue 4, 2014, Pages 1118-1143

Sizing up single-molecule enzymatic conformational dynamics

Author keywords

[No Author keywords available]

Indexed keywords

PROTEIN;

EID: 84893372728     PISSN: 03060012     EISSN: 14604744     Source Type: Journal    
DOI: 10.1039/c3cs60191a     Document Type: Review
Times cited : (60)

References (174)
  • 1
    • 0030003076 scopus 로고    scopus 로고
    • Studies on single alkaline phosphatase molecules: Reaction rate and activation energy of a reaction catalyzed by a single molecule and the effect of thermal denaturation - The death of an enzyme
    • DOI 10.1021/ja9540839
    • D. B. Craig E. A. Arriaga J. C. Y. Wong H. Lu N. J. Dovichi Studies on single alkaline phosphatase molecules: reaction rate and activation energy of a reaction catalyzed by a single molecule and the effect of thermal denaturation-the death of an enzyme J. Am. Chem. Soc. 1996 118 22 5245 5253 (Pubitemid 26201544)
    • (1996) Journal of the American Chemical Society , vol.118 , Issue.22 , pp. 5245-5253
    • Craig, D.B.1    Arriaga, E.A.2    Wong, J.C.Y.3    Lu, H.4    Dovichi, N.J.5
  • 3
    • 33644910749 scopus 로고    scopus 로고
    • Ever-fluctuating single enzyme molecules: Michaelis-Menten equation revisited
    • B. P. English et al., Ever-fluctuating single enzyme molecules: Michaelis-Menten equation revisited Nat. Chem. Biol. 2006 2 2 87 94
    • (2006) Nat. Chem. Biol. , vol.2 , Issue.2 , pp. 87-94
    • English, B.P.1
  • 5
    • 0032484096 scopus 로고    scopus 로고
    • Single-molecule enzymatic dynamics
    • H. P. Lu L. Y. Xun X. S. Xie Single-molecule enzymatic dynamics Science 1998 282 5395 1877 1882 (Pubitemid 28555264)
    • (1998) Science , vol.282 , Issue.5395 , pp. 1877-1882
    • Xie, X.S.1
  • 6
    • 0033523011 scopus 로고    scopus 로고
    • Single-molecule enzymology
    • X. S. Xie H. P. Lu Single-molecule enzymology J. Biol. Chem. 1999 274 23 15967 15970
    • (1999) J. Biol. Chem. , vol.274 , Issue.23 , pp. 15967-15970
    • Xie, X.S.1    Lu, H.P.2
  • 7
    • 0028934277 scopus 로고
    • Differences in the Chemicat-Reactivity of Individual Molecules of an Enzyme
    • Q. F. Xue E. S. Yeung Differences in The Chemicat-Reactivity of Individual Molecules of an Enzyme Nature 1995 373 6516 681 683
    • (1995) Nature , vol.373 , Issue.6516 , pp. 681-683
    • Xue, Q.F.1    Yeung, E.S.2
  • 8
    • 0034248114 scopus 로고    scopus 로고
    • Conformational cycle of a single working enzyme
    • N. Agmon Conformational cycle of a single working enzyme J. Phys. Chem. B 2000 104 32 7830 7834
    • (2000) J. Phys. Chem. B , vol.104 , Issue.32 , pp. 7830-7834
    • Agmon, N.1
  • 9
    • 0042233472 scopus 로고    scopus 로고
    • Probing single-molecule T4 lysozyme conformational dynamics by intramolecular fluorescence energy transfer
    • Y. Chen D. H. Hu E. R. Vorpagel H. P. Lu Probing single-molecule T4 lysozyme conformational dynamics by intramolecular fluorescence energy transfer J. Phys. Chem. B 2003 107 31 7947 7956
    • (2003) J. Phys. Chem. B , vol.107 , Issue.31 , pp. 7947-7956
    • Chen, Y.1    Hu, D.H.2    Vorpagel, E.R.3    Lu, H.P.4
  • 10
    • 0003061529 scopus 로고    scopus 로고
    • Single Molecule Detectionin Life Science
    • Y. Ishii T. Yanagida Single Molecule Detectionin Life Science Single Mol. 2000 1 5 16
    • (2000) Single Mol. , vol.1 , pp. 5-16
    • Ishii, Y.1    Yanagida, T.2
  • 11
    • 57449113389 scopus 로고    scopus 로고
    • Single-molecule DNA damage recognition: DNA-protein protein-protein interaction dynamics
    • H. P. Lu L. M. Iakoucheva E. J. Ackerman Single-molecule DNA damage recognition: DNA-protein protein-protein interaction dynamics Biophys. J. 2000 78 1 262A
    • (2000) Biophys. J. , vol.78 , Issue.1
    • Lu, H.P.1    Iakoucheva, L.M.2    Ackerman, E.J.3
  • 12
    • 0035913704 scopus 로고    scopus 로고
    • Single-molecule conformational dynamics of fluctuating noncovalent DNA-protein interactions in DNA damage recognition [3]
    • DOI 10.1021/ja0058942
    • H. P. Lu L. M. Iakoucheva E. J. Ackerman Single-molecule conformational dynamics of fluctuating noncovalent DNA-Protein interactions a in DNA damage recognition J. Am. Chem. Soc. 2001 123 37 9184 9185 (Pubitemid 32884748)
    • (2001) Journal of the American Chemical Society , vol.123 , Issue.37 , pp. 9184-9185
    • Lu, H.P.1    Iakoucheva, L.M.2    Ackerman, E.J.3
  • 13
    • 0033548657 scopus 로고    scopus 로고
    • Illuminating single molecules in condensed matter
    • W. E. Moerner M. Orrit Illuminating single molecules in condensed matter Science 1999 283 5408 1670 1676
    • (1999) Science , vol.283 , Issue.5408 , pp. 1670-1676
    • Moerner, W.E.1    Orrit, M.2
  • 14
    • 0001248634 scopus 로고    scopus 로고
    • Statistical Analyses and Theoretical Models of Single-Molecule Enzymatic Dynamics
    • G. K. Schenter H. P. Lu X. S. Xie Statistical analyses and theoretical models of single-molecule enzymatic dynamics J. Phys. Chem. A 1999 103 49 10477 10488 (Pubitemid 129571336)
    • (1999) Journal of Physical Chemistry A , vol.103 , Issue.49 , pp. 10477-10488
    • Schenter, G.K.1    Lu, H.P.2    Xie, X.S.3
  • 16
    • 9644263074 scopus 로고
    • Intermittency of Single-Molecule Reaction Dynamics in Fluctuating Environments
    • J. Wang P. Wolynes Intermittency of Single-Molecule Reaction Dynamics in Fluctuating Environments Phys. Rev. Lett. 1995 74 21 4317 4320
    • (1995) Phys. Rev. Lett. , vol.74 , Issue.21 , pp. 4317-4320
    • Wang, J.1    Wolynes, P.2
  • 17
    • 0001468698 scopus 로고    scopus 로고
    • Optical studies of single molecules at room temperature
    • X. S. Xie J. K. Trautman Optical studies of single molecules at room temperature Annu. Rev. Phys. Chem. 1998 49 441 480 (Pubitemid 128436897)
    • (1998) Annual Review of Physical Chemistry , vol.49 , Issue.1 , pp. 441-480
    • Xie, X.S.1    Trautman, J.K.2
  • 18
    • 0001631778 scopus 로고
    • Rate-Processes with Dynamic Disorder
    • R. Zwanzig Rate-Processes with Dynamic Disorder Acc. Chem. Res. 1990 23 5 148 152
    • (1990) Acc. Chem. Res. , vol.23 , Issue.5 , pp. 148-152
    • Zwanzig, R.1
  • 19
    • 29344466944 scopus 로고    scopus 로고
    • Conformation coupled enzyme catalysis: Single-molecule and transient kinetics investigation of dihydrofolate reductase
    • DOI 10.1021/bi051378i
    • N. M. Antikainen R. D. Smiley S. J. Benkovic G. G. Hammes Conformation coupled enzyme catalysis: single-molecule and transient kinetics investigation of dihydrofolate reductase Biochemistry 2005 44 51 16835 16843 (Pubitemid 43007212)
    • (2005) Biochemistry , vol.44 , Issue.51 , pp. 16835-16843
    • Antikainen, N.M.1    Smiley, R.D.2    Benkovic, S.J.3    Hammes, G.G.4
  • 20
    • 0037154884 scopus 로고    scopus 로고
    • Enzyme dynamics during catalysis
    • DOI 10.1126/science.1066176
    • E. Z. Eisenmesser D. A. Bosco M. Akke D. Kern Enzyme dynamics during catalysis Science 2002 295 5559 1520 1523 (Pubitemid 34174006)
    • (2002) Science , vol.295 , Issue.5559 , pp. 1520-1523
    • Eisenmesser, E.Z.1    Bosco, D.A.2    Akke, M.3    Kern, D.4
  • 23
    • 0346726109 scopus 로고    scopus 로고
    • How Enzymes Work: Analysis by Modern Rate Theory and Computer Simulations
    • DOI 10.1126/science.1088172
    • M. Garcia-Viloca J. Gao M. Karplus D. G. Truhlar How enzymes work: analysis by modern rate theory and computer simulations Science 2004 303 5655 186 195 (Pubitemid 38057561)
    • (2004) Science , vol.303 , Issue.5655 , pp. 186-195
    • Garcia-Viloca, M.1    Gao, J.2    Karplus, M.3    Truhlar, D.G.4
  • 25
    • 0033514435 scopus 로고    scopus 로고
    • Single-molecule fluorescence spectroscopy of enzyme conformational dynamics and cleavage mechanism
    • T. J. Ha et al., Single-molecule fluorescence spectroscopy of enzyme conformational dynamics and cleavage mechanism Proc. Natl. Acad. Sci. U. S. A. 1999 96 3 893 898
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , Issue.3 , pp. 893-898
    • Ha, T.J.1
  • 27
    • 0037287425 scopus 로고    scopus 로고
    • Molecular motors and single-molecule enzymology
    • DOI 10.1016/S0076-6879(03)61014-1
    • Y. Ishii K. Kitamura H. Tanaka T. Yanagida Molecular motors and single-molecule enzymology Biophotonics, Pt B 2003 361 228 245 (Pubitemid 36241002)
    • (2003) Methods in Enzymology , vol.361 , pp. 228-245
    • Ishii, Y.1    Kitamura, K.2    Tanaka, H.3    Yanagida, T.4
  • 29
    • 23744506663 scopus 로고    scopus 로고
    • Probing single-molecule protein conformational dynamics
    • DOI 10.1021/ar0401451
    • H. P. Lu Probing single-molecule protein conformational dynamics Acc. Chem. Res. 2005 38 7 557 565 (Pubitemid 41128408)
    • (2005) Accounts of Chemical Research , vol.38 , Issue.7 , pp. 557-565
    • Lu, H.P.1
  • 30
    • 30944460113 scopus 로고    scopus 로고
    • Fluctuating enzymes: Ressons from single-molecule studies
    • W. Min et al., Fluctuating enzymes: ressons from single-molecule studies Acc. Chem. Res. 2005 38 12 923 931
    • (2005) Acc. Chem. Res. , vol.38 , Issue.12 , pp. 923-931
    • Min, W.1
  • 31
    • 69149090263 scopus 로고    scopus 로고
    • Role of conformational dynamics in kinetics of an enzymatic cycle in a nonequilibrium steady state
    • W. Min X. S. Xie B. Bagchi Role of conformational dynamics in kinetics of an enzymatic cycle in a nonequilibrium steady state J. Chem. Phys. 2009 131 6 065104
    • (2009) J. Chem. Phys. , vol.131 , Issue.6 , pp. 065104
    • Min, W.1    Xie, X.S.2    Bagchi, B.3
  • 32
    • 76649114676 scopus 로고    scopus 로고
    • Protein dynamics and conformational disorder in molecular recognition
    • T. Mittag L. E. Kay J. D. Forman-Kay Protein dynamics and conformational disorder in molecular recognition J. Mol. Recognit. 2009 23 2 105 116
    • (2009) J. Mol. Recognit. , vol.23 , Issue.2 , pp. 105-116
    • Mittag, T.1    Kay, L.E.2    Forman-Kay, J.D.3
  • 34
    • 0141993723 scopus 로고    scopus 로고
    • The motions of an enzyme soloist
    • DOI 10.1126/science.1090850
    • M. Orrit The motions of an enzyme soloist Science 2003 302 5643 239 240 (Pubitemid 37248744)
    • (2003) Science , vol.302 , Issue.5643 , pp. 239-240
    • Orrit, M.1
  • 35
    • 70350453758 scopus 로고    scopus 로고
    • Enzyme millisecond conformational dynamics do not catalyze the chemical step
    • A. V. Pisliakov J. Cao S. C. L. Kamerlin A. Warshel Enzyme millisecond conformational dynamics do not catalyze the chemical step Proc. Natl. Acad. Sci. U. S. A. 2009 106 41 17359 17364
    • (2009) Proc. Natl. Acad. Sci. U. S. A. , vol.106 , Issue.41 , pp. 17359-17364
    • Pisliakov, A.V.1    Cao, J.2    Kamerlin, S.C.L.3    Warshel, A.4
  • 37
    • 0035976603 scopus 로고    scopus 로고
    • Real-time single-molecule imaging of the infection pathway of anadeno-associated virus
    • DOI 10.1126/science.1064103
    • G. Seisenberger et al., Real-time single-molecule imaging of the infection pathway of an adeno-associated virus Science 2001 294 5548 1929 1932 (Pubitemid 33101590)
    • (2001) Science , vol.294 , Issue.5548 , pp. 1929-1932
    • Seisenberger, G.1    Ried, M.U.2    Endress, T.3    Buning, H.4    Hallek, M.5    Brauchle, C.6
  • 38
    • 0033536183 scopus 로고    scopus 로고
    • Single kinesin molecules studied with a molecular force clamp
    • DOI 10.1038/22146
    • K. Visscher M. J. Schnitzer S. M. Block Single kinesin molecules studied with a molecular force clamp Nature 1999 400 6740 184 189 (Pubitemid 29327550)
    • (1999) Nature , vol.400 , Issue.6740 , pp. 184-189
    • Visscher, K.1    Schnltzer, M.J.2    Block, S.M.3
  • 39
    • 61949448788 scopus 로고    scopus 로고
    • Energy landscape along an enzymatic reaction trajectory: Hinges or cracks?
    • P. C. Whitford J. N. Onuchic P. G. Wolynes Energy landscape along an enzymatic reaction trajectory: hinges or cracks? HFSP J. 2008 2 2 61 64
    • (2008) HFSP J. , vol.2 , Issue.2 , pp. 61-64
    • Whitford, P.C.1    Onuchic, J.N.2    Wolynes, P.G.3
  • 42
    • 0026320866 scopus 로고
    • The energy landscapes and motions of proteins
    • H. Frauenfelder S. G. Sligar P. G. Wolynes The energy landscapes and motions of proteins Science 1991 254 5038 1598 1603 (Pubitemid 21917496)
    • (1991) Science , vol.254 , Issue.5038 , pp. 1598-1603
    • Frauenfelder, H.1    Sligar, S.G.2    Wolynes, P.G.3
  • 44
    • 80052570717 scopus 로고    scopus 로고
    • Probing Single-Molecule Enzyme Active-Site Conformational State Intermittent Coherence
    • Y. He et al., Probing Single-Molecule Enzyme Active-Site Conformational State Intermittent Coherence J. Am. Chem. Soc. 2011 133 36 14389 14395
    • (2011) J. Am. Chem. Soc. , vol.133 , Issue.36 , pp. 14389-14395
    • He, Y.1
  • 45
    • 84857698151 scopus 로고    scopus 로고
    • Manipulating Protein Conformations by Single-Molecule AFM-FRET Nanoscopy
    • Y. He M. Lu J. Cao H. P. Lu Manipulating Protein Conformations by Single-Molecule AFM-FRET Nanoscopy ACS Nano 2012 6 2 1221 1229
    • (2012) ACS Nano , vol.6 , Issue.2 , pp. 1221-1229
    • He, Y.1    Lu, M.2    Cao, J.3    Lu, H.P.4
  • 46
    • 84871334568 scopus 로고    scopus 로고
    • Single-molecule photon stamping FRET spectroscopy study of enzymatic conformational dynamics
    • Y. He M. Lu H. P. Lu Single-molecule photon stamping FRET spectroscopy study of enzymatic conformational dynamics Phys. Chem. Chem. Phys. 2013 15 3 770 775
    • (2013) Phys. Chem. Chem. Phys. , vol.15 , Issue.3 , pp. 770-775
    • He, Y.1    Lu, M.2    Lu, H.P.3
  • 47
    • 84856077205 scopus 로고    scopus 로고
    • Enzymes in Coherent Motion
    • H. P. Lu Enzymes in Coherent Motion Science 2012 335 6066 300 301
    • (2012) Science , vol.335 , Issue.6066 , pp. 300-301
    • Lu, H.P.1
  • 49
    • 3042735586 scopus 로고    scopus 로고
    • Placing single-molecule T4 lysozyme enzymes on a bacterial cell surface: Toward probing single-molecule enzymatic reaction in living cells
    • DOI 10.1529/biophysj.104.042101
    • D. H. Hu H. P. Lu Placing single-molecule T4 lysozyme enzymes on a bacterial cell surface: toward probing single-molecule enzymatic reaction in living cells Biophys. J. 2004 87 1 656 661 (Pubitemid 38880118)
    • (2004) Biophysical Journal , vol.87 , Issue.1 , pp. 656-661
    • Hu, D.1    Lu, H.P.2
  • 50
    • 33746969931 scopus 로고    scopus 로고
    • Revealing two-state protein-protein interactions of calmodulin by single-molecule spectroscopy
    • DOI 10.1021/ja057005m
    • R. C. Liu D. H. Hu X. Tan H. P. Lu Revealing two-state protein-protein interactions of calmodulin by single-molecule spectroscopy J. Am. Chem. Soc. 2006 128 31 10034 10042 (Pubitemid 44202174)
    • (2006) Journal of the American Chemical Society , vol.128 , Issue.31 , pp. 10034-10042
    • Liu, R.1    Hu, D.2    Tan, X.3    Lu, H.P.4
  • 51
    • 3042585198 scopus 로고    scopus 로고
    • Single-molecule spectroscopy studies of conformational change dynamics in enzymatic reactions
    • DOI 10.2174/1389201043376887
    • H. P. Lu Single-molecule spectroscopy studies of conformational change dynamics in enzymatic reactions Curr. Pharm. Biotechnol. 2004 5 3 261 269 (Pubitemid 38821331)
    • (2004) Current Pharmaceutical Biotechnology , vol.5 , Issue.3 , pp. 261-269
    • Lu, H.P.1
  • 52
    • 59049099584 scopus 로고    scopus 로고
    • Combined Single-Molecule Electrical Recording and Single-Molecule Spectroscopy Studies of Ion Channel Conformational Dynamics
    • ed. B. Jena
    • H. P. Lu, Combined Single-Molecule Electrical Recording and Single-Molecule Spectroscopy Studies of Ion Channel Conformational Dynamics, in Methods in Nano Cell Biology, ed., B. P. Jena, 2008, vol. 90, pp. 435-451
    • (2008) Methods in Nano Cell Biology , vol.90 , pp. 435-451
    • Lu, H.P.1
  • 53
    • 70350482712 scopus 로고    scopus 로고
    • Single-Molecule Protein Interaction Conformational Dynamics
    • H. P. Lu Single-Molecule Protein Interaction Conformational Dynamics Curr. Pharm. Biotechnol. 2009 10 5 522 531
    • (2009) Curr. Pharm. Biotechnol. , vol.10 , Issue.5 , pp. 522-531
    • Lu, H.P.1
  • 54
    • 78650255430 scopus 로고    scopus 로고
    • Single-Molecule Protein Conformational Dynamics in Enzymatic Reactions
    • ed. A. Graslund, R. Rigler and J. Widengren
    • H. P. Lu, Single-Molecule Protein Conformational Dynamics in Enzymatic Reactions, in Single Molecule Spectroscopy in Chemistry, Physics and Biology, ed., A. Graslund, R. Rigler, and, J. Widengren, 2010, vol. 96, pp. 471-494
    • (2010) Single Molecule Spectroscopy in Chemistry, Physics and Biology , vol.96 , pp. 471-494
    • Lu, H.P.1
  • 55
    • 79953329022 scopus 로고    scopus 로고
    • Revealing time bunching effect in single-molecule enzyme conformational dynamics
    • H. P. Lu Revealing time bunching effect in single-molecule enzyme conformational dynamics Phys. Chem. Chem. Phys. 2011 13 15 6734 6749
    • (2011) Phys. Chem. Chem. Phys. , vol.13 , Issue.15 , pp. 6734-6749
    • Lu, H.P.1
  • 56
    • 33947586778 scopus 로고    scopus 로고
    • Exploring the mechanism of flexible biomolecular recognition with single molecule dynamics
    • Q. Lu H. P. Lu J. Wang Exploring the mechanism of flexible biomolecular recognition with single molecule dynamics Phys. Rev. Lett. 2007 98 12 128105
    • (2007) Phys. Rev. Lett. , vol.98 , Issue.12 , pp. 128105
    • Lu, Q.1    Lu, H.P.2    Wang, J.3
  • 57
    • 77952477639 scopus 로고    scopus 로고
    • Bunching Effect in Single-Molecule T4 Lysozyme Nonequilibrium Conformational Dynamics under Enzymatic Reactions
    • Y. M. Wang H. P. Lu Bunching Effect in Single-Molecule T4 Lysozyme Nonequilibrium Conformational Dynamics under Enzymatic Reactions J. Phys. Chem. B 2010 114 19 6669 6674
    • (2010) J. Phys. Chem. B , vol.114 , Issue.19 , pp. 6669-6674
    • Wang, Y.M.1    Lu, H.P.2
  • 58
    • 21344431829 scopus 로고    scopus 로고
    • Single-molecule study of protein-protein and protein-DNA interaction dynamics
    • ed. G. U. Nienhaus
    • H. P. Lu, Single-molecule study of protein-protein and protein-DNA interaction dynamics, in Methods in Molecular Biology, ed., G. U. Nienhaus, 2005, vol. 305, pp. 385-413
    • (2005) Methods in Molecular Biology , vol.305 , pp. 385-413
    • Lu, H.P.1
  • 59
    • 1642485194 scopus 로고    scopus 로고
    • Single-molecule study of protein-protein interaction dynamics in a cell signaling system
    • X. Tan et al., Single-molecule study of protein-protein interaction dynamics in a cell signaling system J. Phys. Chem. B 2004 108 2 737 744
    • (2004) J. Phys. Chem. B , vol.108 , Issue.2 , pp. 737-744
    • Tan, X.1
  • 60
    • 33746607765 scopus 로고    scopus 로고
    • Single-molecule dynamics reveals cooperative binding-folding in protein recognition
    • J. Wang Q. Lu H. P. Lu Single-molecule dynamics reveals cooperative binding-folding in protein recognition PLoS Comput. Biol. 2006 2 7 842 852
    • (2006) PLoS Comput. Biol. , vol.2 , Issue.7 , pp. 842-852
    • Wang, J.1    Lu, Q.2    Lu, H.P.3
  • 61
    • 57449089615 scopus 로고    scopus 로고
    • 2D Regional Correlation Analysis of Single-Molecule Time Trajectories
    • X. Wang H. P. Lu 2D Regional Correlation Analysis of Single-Molecule Time Trajectories J. Phys. Chem. B 2008 112 47 14920 14926
    • (2008) J. Phys. Chem. B , vol.112 , Issue.47 , pp. 14920-14926
    • Wang, X.1    Lu, H.P.2
  • 62
    • 84873647198 scopus 로고    scopus 로고
    • Probing Allostery Through DNA
    • S. Kim et al., Probing Allostery Through DNA Science 2013 339 6121 816 819
    • (2013) Science , vol.339 , Issue.6121 , pp. 816-819
    • Kim, S.1
  • 63
    • 77951770226 scopus 로고    scopus 로고
    • Complex Kinetics of Fluctuating Enzymes: Phase Diagram Characterization of a Minimal Kinetic Scheme
    • W. Min L. Jiang X. S. Xie Complex Kinetics of Fluctuating Enzymes: Phase Diagram Characterization of a Minimal Kinetic Scheme Chem.-Asian J. 2010 5 5 1129 1138
    • (2010) Chem.-Asian J. , vol.5 , Issue.5 , pp. 1129-1138
    • Min, W.1    Jiang, L.2    Xie, X.S.3
  • 64
    • 38749105098 scopus 로고    scopus 로고
    • Two-dimensional reaction free energy surfaces of catalytic reaction: Effects of protein conformational dynamics on enzyme catalysis
    • DOI 10.1021/jp076533c
    • W. Min X. S. Xie B. Bagchi Two-dimensional reaction free energy surfaces of catalytic reaction: effects of protein conformational dynamics on enzyme catalysis J. Phys. Chem. B 2008 112 2 454 466 (Pubitemid 351184620)
    • (2008) Journal of Physical Chemistry B , vol.112 , Issue.2 , pp. 454-466
    • Min, W.1    Xie, X.S.2    Bagchi, B.3
  • 65
    • 78650216327 scopus 로고    scopus 로고
    • Enzymology and Life at the Single Molecule Level
    • ed. A. Graslund, R. Rigler and J. Widengren
    • X. S. Xie, Enzymology and Life at the Single Molecule Level, in Single Molecule Spectroscopy in Chemistry, Physics and Biology, ed., A. Graslund, R. Rigler, and, J. Widengren, 2010, vol. 96, pp. 435-448
    • (2010) Single Molecule Spectroscopy in Chemistry, Physics and Biology , vol.96 , pp. 435-448
    • Xie, X.S.1
  • 66
    • 84856073680 scopus 로고    scopus 로고
    • Single-Molecule Lysozyme Dynamics Monitored by an Electronic Circuit
    • Y. Choi et al., Single-Molecule Lysozyme Dynamics Monitored by an Electronic Circuit Science 2012 335 6066 319 324
    • (2012) Science , vol.335 , Issue.6066 , pp. 319-324
    • Choi, Y.1
  • 67
    • 84856461531 scopus 로고    scopus 로고
    • Single-Molecule Dynamics of Lysozyme Processing Distinguishes Linear and Cross-Linked Peptidoglycan Substrates
    • Y. Choi et al., Single-Molecule Dynamics of Lysozyme Processing Distinguishes Linear and Cross-Linked Peptidoglycan Substrates J. Am. Chem. Soc. 2012 134 4 2032 2035
    • (2012) J. Am. Chem. Soc. , vol.134 , Issue.4 , pp. 2032-2035
    • Choi, Y.1
  • 68
    • 84873629244 scopus 로고    scopus 로고
    • Dissecting Single-Molecule Signal Transduction in Carbon Nanotube Circuits with Protein Engineering
    • Y. Choi et al., Dissecting Single-Molecule Signal Transduction in Carbon Nanotube Circuits with Protein Engineering Nano Lett. 2013 13 2 625 631
    • (2013) Nano Lett. , vol.13 , Issue.2 , pp. 625-631
    • Choi, Y.1
  • 69
    • 84878392485 scopus 로고    scopus 로고
    • Electronic Measurements of Single-Molecule Catalysis by cAMP-Dependent Protein Kinase A
    • P. C. Sims et al., Electronic Measurements of Single-Molecule Catalysis by cAMP-Dependent Protein Kinase A J. Am. Chem. Soc. 2013 135 21 7861 7868
    • (2013) J. Am. Chem. Soc. , vol.135 , Issue.21 , pp. 7861-7868
    • Sims, P.C.1
  • 71
    • 0016624901 scopus 로고
    • Binding-Energy, Specificity, and Enzymic Catalysis-Circe Effect
    • W. P. Jencks Binding-Energy, Specificity, and Enzymic Catalysis-Circe Effect Adv. Enzymol. Relat. Areas Mol. Biol. 1975 43 219 410
    • (1975) Adv. Enzymol. Relat. Areas Mol. Biol. , vol.43 , pp. 219-410
    • Jencks, W.P.1
  • 72
    • 24644483073 scopus 로고    scopus 로고
    • Large amplitude conformational change in proteins explored with a plastic network model: Adenylate kinase
    • DOI 10.1016/j.jmb.2005.07.031, PII S0022283605008193
    • P. Maragakis M. Karplus Large amplitude conformational change in proteins explored with a plastic network model: adenylate kinase J. Mol. Biol. 2005 352 4 807 822 (Pubitemid 41267070)
    • (2005) Journal of Molecular Biology , vol.352 , Issue.4 , pp. 807-822
    • Maragakis, P.1    Karplus, M.2
  • 74
    • 84861380340 scopus 로고    scopus 로고
    • Single-Molecule Mechanoenzymatics
    • ed. D. C. Rees
    • E. M. Puchner and H. E. Gaub, Single-Molecule Mechanoenzymatics, in Annu Rev Biophys, ed., D. C. Rees, 2012, vol. 41, pp. 497-518
    • (2012) Annu Rev Biophys , vol.41 , pp. 497-518
    • Puchner, E.M.1    Gaub, H.E.2
  • 75
    • 0029644728 scopus 로고
    • Movie of the Structural-Changes during a catalytic Cycle of Nucleoside Monophosphate Kinases
    • C. Vonrhein G. J. Schlauderer G. E. Schulz Movie of The Structural-Changes During a catalytic Cycle of Nucleoside Monophosphate Kinases Structure 1995 3 5 483 490
    • (1995) Structure , vol.3 , Issue.5 , pp. 483-490
    • Vonrhein, C.1    Schlauderer, G.J.2    Schulz, G.E.3
  • 76
    • 17644435744 scopus 로고    scopus 로고
    • Nucleoside monophosphate kinases: Structure, mechanism, and substrate specificity
    • H. G. Yan M. D. Tsai Nucleoside monophosphate kinases: structure, mechanism, and substrate specificity Adv. Enzymol. 1999 73 103 134
    • (1999) Adv. Enzymol. , vol.73 , pp. 103-134
    • Yan, H.G.1    Tsai, M.D.2
  • 77
    • 0034674420 scopus 로고    scopus 로고
    • A single-molecule study of RNA catalysis and folding
    • X. W. Zhuang et al., A single-molecule study of RNA catalysis and folding Science 2000 288 5473 2048 2051
    • (2000) Science , vol.288 , Issue.5473 , pp. 2048-2051
    • Zhuang, X.W.1
  • 78
    • 0024280869 scopus 로고
    • Structure and Function of Voltage-Sensitive Ion Channels
    • W. A. Catterall Structure and Function of Voltage-Sensitive Ion Channels Science 1988 242 4875 50 61
    • (1988) Science , vol.242 , Issue.4875 , pp. 50-61
    • Catterall, W.A.1
  • 81
    • 84861216803 scopus 로고    scopus 로고
    • Theory of the energy transfer efficiency and fluorescence lifetime distribution in single-molecule FRET
    • I. V. Gopich A. Szabo Theory of the energy transfer efficiency and fluorescence lifetime distribution in single-molecule FRET Proc. Natl. Acad. Sci. U. S. A. 2012 109 20 7747 7752
    • (2012) Proc. Natl. Acad. Sci. U. S. A. , vol.109 , Issue.20 , pp. 7747-7752
    • Gopich, I.V.1    Szabo, A.2
  • 82
    • 70349961707 scopus 로고    scopus 로고
    • Triggering Enzymatic Activity with Force
    • H. Gumpp et al., Triggering Enzymatic Activity with Force Nano Lett. 2009 9 9 3290 3295
    • (2009) Nano Lett. , vol.9 , Issue.9 , pp. 3290-3295
    • Gumpp, H.1
  • 84
    • 18744389451 scopus 로고    scopus 로고
    • The study of protein folding and dynamics by determination of intramolecular distance distributions and their fluctuations using ensemble and single-molecule FRET measurements
    • DOI 10.1002/cphc.200400617
    • E. Haas The study of protein folding and dynamics by determination of intramolecular distance distributions and their fluctuations using ensemble and single-molecule FRET measurements ChemPhysChem 2005 6 5 858 870 (Pubitemid 40669549)
    • (2005) ChemPhysChem , vol.6 , Issue.5 , pp. 858-870
    • Haas, E.1
  • 85
    • 1842424308 scopus 로고    scopus 로고
    • Probing ion channel conformational dynamics using simultaneous single-molecule ultrafast spectroscopy and patch-clamp electric recording
    • G. Harms G. Orr H. P. Lu Probing ion channel conformational dynamics using simultaneous single-molecule ultrafast spectroscopy and patch-clamp electric recording Appl. Phys. Lett. 2004 84 10 1792 1794
    • (2004) Appl. Phys. Lett. , vol.84 , Issue.10 , pp. 1792-1794
    • Harms, G.1    Orr, G.2    Lu, H.P.3
  • 86
    • 0041821419 scopus 로고    scopus 로고
    • Probing conformational changes of gramicidin ion channels by single-molecule patch-clamp fluorescence microscopy
    • G. S. Harms et al., Probing conformational changes of gramicidin ion channels by single-molecule patch-clamp fluorescence microscopy Biophys. J. 2003 85 3 1826 1838 (Pubitemid 37052264)
    • (2003) Biophysical Journal , vol.85 , Issue.3 , pp. 1826-1838
    • Harms, G.S.1    Orr, G.2    Montal, M.3    Thrall, B.D.4    Colson, S.D.5    Lu, H.P.6
  • 87
    • 0003443746 scopus 로고
    • Sinauer Associates, Inc., Sunderland, Massachusetts USA., 2nd edn
    • B. Hille, Ionic Channels of Excitable Membranes, Sinauer Associates, Inc., Sunderland, Massachusetts USA., 2nd edn, 1992
    • (1992) Ionic Channels of Excitable Membranes
    • Hille, B.1
  • 89
    • 84859651420 scopus 로고    scopus 로고
    • Mechanism of Voltage Gating in Potassium Channels
    • M. O. Jensen et al., Mechanism of Voltage Gating in Potassium Channels Science 2012 336 6078 229 233
    • (2012) Science , vol.336 , Issue.6078 , pp. 229-233
    • Jensen, M.O.1
  • 90
    • 0033462513 scopus 로고    scopus 로고
    • Folding dynamics of single GCN4 peptides by fluorescence resonant energy transfer confocal microscopy
    • Y. W. Jia et al., Folding dynamics of single GCN4 peptides by fluorescence resonant energy transfer confocal microscopy Chem. Phys. 1999 247 1 69 83
    • (1999) Chem. Phys. , vol.247 , Issue.1 , pp. 69-83
    • Jia, Y.W.1
  • 91
    • 70149120516 scopus 로고    scopus 로고
    • Single-molecule force spectroscopy distinguishes target binding modes of calmodulin
    • J. P. Junker M. Rief Single-molecule force spectroscopy distinguishes target binding modes of calmodulin Proc. Natl. Acad. Sci. U. S. A. 2009 106 34 14361 14366
    • (2009) Proc. Natl. Acad. Sci. U. S. A. , vol.106 , Issue.34 , pp. 14361-14366
    • Junker, J.P.1    Rief, M.2
  • 92
    • 59149096062 scopus 로고    scopus 로고
    • Ligand-Dependent Equilibrium Fluctuations of Single Calmodulin Molecules
    • J. P. Junker F. Ziegler M. Rief Ligand-Dependent Equilibrium Fluctuations of Single Calmodulin Molecules Science 2009 323 5914 633 637
    • (2009) Science , vol.323 , Issue.5914 , pp. 633-637
    • Junker, J.P.1    Ziegler, F.2    Rief, M.3
  • 93
    • 77953415522 scopus 로고    scopus 로고
    • Detection of Structural Dynamics by FRET: A Photon Distribution and Fluorescence Lifetime Analysis of Systems with Multiple States
    • S. Kalinin A. Valeri M. Antonik S. Felekyan C. A. M. Seidel Detection of Structural Dynamics by FRET: A Photon Distribution and Fluorescence Lifetime Analysis of Systems with Multiple States J. Phys. Chem. B 2010 114 23 7983 7995
    • (2010) J. Phys. Chem. B , vol.114 , Issue.23 , pp. 7983-7995
    • Kalinin, S.1    Valeri, A.2    Antonik, M.3    Felekyan, S.4    Seidel, C.A.M.5
  • 95
    • 13644273766 scopus 로고    scopus 로고
    • Mechanical perturbation-induced fluorescence change of green fluorescent protein
    • T. Kodama H. Ohtani H. Arakawa A. Ikai Mechanical perturbation-induced fluorescence change of green fluorescent protein Appl. Phys. Lett. 2005 86 4 043901
    • (2005) Appl. Phys. Lett. , vol.86 , Issue.4 , pp. 043901
    • Kodama, T.1    Ohtani, H.2    Arakawa, H.3    Ikai, A.4
  • 96
    • 0027730754 scopus 로고
    • A covalent enzyme-substrate intermediate with saccharide distortion in a mutant T4 lysozyme
    • R. Kuroki L. H. Weaver B. W. Matthews A Covalent Enzyme-Substrate Intermediate with Saccharide Distortion in a Mutant T4 Lysozyme Science 1993 262 5142 2030 2033 (Pubitemid 24041881)
    • (1993) Science , vol.262 , Issue.5142 , pp. 2030-2033
    • Kuroki, R.1    Weaver, L.H.2    Matthews, B.W.3
  • 98
    • 23644433196 scopus 로고    scopus 로고
    • Measurements of internal distance changes of the 30 S ribosome using FRET with multiple donor-acceptor pairs: Quantitative spectroscopic methods
    • DOI 10.1016/j.jmb.2005.06.027, PII S0022283605006777
    • Z. K. Majumdar R. Hickerson H. F. Noller R. M. Clegg Measurements of internal distance changes of the 30 S ribosome using FRET with multiple donor-acceptor pairs: quantitative spectroscopic methods J. Mol. Biol. 2005 351 5 1123 1145 (Pubitemid 41133457)
    • (2005) Journal of Molecular Biology , vol.351 , Issue.5 , pp. 1123-1145
    • Majumdar, Z.K.1    Hickerson, R.2    Noller, H.F.3    Clegg, R.M.4
  • 99
    • 0028968018 scopus 로고
    • Study on Protein Stability with T4 Lysozyme
    • B. W. Matthews Study on Protein Stability with T4 Lysozyme Adv. Protein. Chem. 1995 46 249 278
    • (1995) Adv. Protein. Chem. , vol.46 , pp. 249-278
    • Matthews, B.W.1
  • 100
    • 0019421683 scopus 로고
    • Gated binding of ligands to proteins
    • DOI 10.1038/293316a0
    • J. A. McCammon S. H. Northrup Gated Binding of Ligands to Proteins Nature 1981 293 5830 316 317 (Pubitemid 11016269)
    • (1981) Nature , vol.293 , Issue.5830 , pp. 316-317
    • McCammon, J.A.1    Northrup, S.H.2
  • 102
    • 44449134820 scopus 로고    scopus 로고
    • A practical guide to single-molecule FRET
    • DOI 10.1038/nmeth.1208, PII NMETH.1208
    • R. Roy S. Hohng T. Ha A practical guide to single-molecule FRET Nat. Methods 2008 5 6 507 516 (Pubitemid 351761757)
    • (2008) Nature Methods , vol.5 , Issue.6 , pp. 507-516
    • Roy, R.1    Hohng, S.2    Ha, T.3
  • 104
    • 0037126290 scopus 로고    scopus 로고
    • Probing the free-energy surface for protein folding with single-molecule fluorescence spectroscopy
    • DOI 10.1038/nature01060
    • B. Schuler E. A. Lipman W. A. Eaton Probing the free-energy surface for protein folding with single-molecule fluorescence spectroscopy Nature 2002 419 6908 743 747 (Pubitemid 35177962)
    • (2002) Nature , vol.419 , Issue.6908 , pp. 743-747
    • Schuler, B.1    Lipman, E.A.2    Eaton, W.A.3
  • 106
    • 1542501215 scopus 로고    scopus 로고
    • Dynamics and folding of single two-stranded coiled-coil peptides studied by fluorescent energy transfer confocal microscopy
    • D. S. Talaga et al., Dynamics and folding of single two-stranded coiled-coil peptides studied by fluorescent energy transfer confocal microscopy Proc. Natl. Acad. Sci. U. S. A. 2000 97 24 13021 13026
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , Issue.24 , pp. 13021-13026
    • Talaga, D.S.1
  • 107
    • 33645241242 scopus 로고    scopus 로고
    • Single-molecule detection and identification of multiple species by multiparameter fluorescence detection
    • J. Widengren et al., Single-molecule detection and identification of multiple species by multiparameter fluorescence detection Anal. Chem. 2006 78 6 2039 2050
    • (2006) Anal. Chem. , vol.78 , Issue.6 , pp. 2039-2050
    • Widengren, J.1
  • 109
    • 0037461522 scopus 로고    scopus 로고
    • Probing single-molecule dynamics photon by photon
    • H. Yang X. S. Xie Probing single-molecule dynamics photon by photon J. Chem. Phys. 2002 117 24 10965 10979
    • (2002) J. Chem. Phys. , vol.117 , Issue.24 , pp. 10965-10979
    • Yang, H.1    Xie, X.S.2
  • 110
    • 33947517676 scopus 로고    scopus 로고
    • A survey of single-molecule techniques in chemical biology
    • DOI 10.1021/cb600342a
    • P. V. Cornish T. Ha A survey of single-molecule techniques in chemical biology ACS Chem. Biol. 2007 2 1 53 61 (Pubitemid 47490242)
    • (2007) ACS Chemical Biology , vol.2 , Issue.1 , pp. 53-61
    • Cornish, P.V.1    Ha, T.2
  • 111
  • 112
    • 23744433971 scopus 로고    scopus 로고
    • Surfaces and Orientations: Much to FRET about?
    • DOI 10.1021/ar040138c
    • I. Rasnik S. A. McKinney T. Ha Surfaces and orientations: much to FRET about? Acc. Chem. Res. 2005 38 7 542 548 (Pubitemid 41128406)
    • (2005) Accounts of Chemical Research , vol.38 , Issue.7 , pp. 542-548
    • Rasnik, I.1    McKinney, S.A.2    Ha, T.3
  • 113
    • 67650507150 scopus 로고    scopus 로고
    • Fluorescent Lifetime Trajectories of a Single Fluorophore Reveal Reaction Intermediates during Transcription Initiation
    • M. Sorokina H.-R. Koh S. S. Patel T. Ha Fluorescent Lifetime Trajectories of a Single Fluorophore Reveal Reaction Intermediates During Transcription Initiation J. Am. Chem. Soc. 2009 131 28 9630 9631
    • (2009) J. Am. Chem. Soc. , vol.131 , Issue.28 , pp. 9630-9631
    • Sorokina, M.1    Koh, H.-R.2    Patel, S.S.3    Ha, T.4
  • 115
    • 33748781457 scopus 로고    scopus 로고
    • The dynamic energy landscape of dihydrofolate reductase catalysis
    • DOI 10.1126/science.1130258
    • D. D. Boehr D. McElheny H. J. Dyson P. E. Wright The dynamic energy landscape of dihydrofolate reductase catalysis Science 2006 313 5793 1638 1642 (Pubitemid 44414038)
    • (2006) Science , vol.313 , Issue.5793 , pp. 1638-1642
    • Boehr, D.D.1    McElheny, D.2    Dyson, H.J.3    Wrightt, P.E.4
  • 116
    • 15844366268 scopus 로고    scopus 로고
    • 15N NMR relaxation
    • DOI 10.1016/j.jmr.2005.01.008, PII S109078070500011X
    • S. L. Chang N. Tjandra Temperature dependence of protein backbone motion from carbonyl C-13 and amide N-15 NMR relaxation J. Magn. Reson. 2005 174 1 43 53 (Pubitemid 40423607)
    • (2005) Journal of Magnetic Resonance , vol.174 , Issue.1 , pp. 43-53
    • Chang, S.-L.1    Tjandra, N.2
  • 117
    • 36849039429 scopus 로고    scopus 로고
    • A hierarchy of timescales in protein dynamics is linked to enzyme catalysis
    • DOI 10.1038/nature06407, PII NATURE06407
    • K. A. Henzler-Wildman et al., A hierarchy of timescales in protein dynamics is linked to enzyme catalysis Nature 2007 450 7171 913 916 (Pubitemid 350231333)
    • (2007) Nature , vol.450 , Issue.7171 , pp. 913-916
    • Henzler-Wildman, K.A.1    Lei, M.2    Thai, V.3    Kerns, S.J.4    Karplus, M.5    Kern, D.6
  • 118
    • 0029000872 scopus 로고
    • Dynamics of the Flexible Loop of Triosephosphate Isomerase -The Loop Motion is not Ligand-Gated
    • J. C. Williams A. E. McDermott Dynamics of The Flexible Loop of Triosephosphate Isomerase -The Loop Motion is not Ligand-Gated Biochemistry 1995 34 26 8309 8319
    • (1995) Biochemistry , vol.34 , Issue.26 , pp. 8309-8319
    • Williams, J.C.1    McDermott, A.E.2
  • 120
    • 33748619206 scopus 로고    scopus 로고
    • An NMR perspective on enzyme dynamics
    • DOI 10.1021/cr050312q
    • D. D. Boehr H. J. Dyson P. E. Wright An NMR perspective on enzyme dynamics Chem. Rev. 2006 106 8 3055 3079 (Pubitemid 44376926)
    • (2006) Chemical Reviews , vol.106 , Issue.8 , pp. 3055-3079
    • Boehr, D.D.1    Dyson, H.J.2    Wright, P.E.3
  • 121
    • 34247341250 scopus 로고    scopus 로고
    • Manipulating single enzymes by an external harmonic force
    • M. A. Lomholt M. Urbakh R. Metzler J. Klafter Manipulating single enzymes by an external harmonic force Phys. Rev. Lett. 2007 98 16 168302
    • (2007) Phys. Rev. Lett. , vol.98 , Issue.16 , pp. 168302
    • Lomholt, M.A.1    Urbakh, M.2    Metzler, R.3    Klafter, J.4
  • 122
    • 70449769332 scopus 로고    scopus 로고
    • Observing biological dynamics at atomic resolution using NMR
    • A. K. Mittermaier L. E. Kay Observing biological dynamics at atomic resolution using NMR Trends Biochem. Sci. 2009 34 12 601 611
    • (2009) Trends Biochem. Sci. , vol.34 , Issue.12 , pp. 601-611
    • Mittermaier, A.K.1    Kay, L.E.2
  • 125
    • 56149118370 scopus 로고    scopus 로고
    • Super-resolution imaging in live Caulobacter crescentus cells using photoswitchable EYFP
    • J. S. Biteen et al., Super-resolution imaging in live Caulobacter crescentus cells using photoswitchable EYFP Nat. Methods 2008 5 11 947 949
    • (2008) Nat. Methods , vol.5 , Issue.11 , pp. 947-949
    • Biteen, J.S.1
  • 126
    • 33645223271 scopus 로고    scopus 로고
    • Suppressing Brownian motion of individual biomolecules in solution
    • A. E. Cohen W. E. Moerner Suppressing Brownian motion of individual biomolecules in solution Proc. Natl. Acad. Sci. U. S. A. 2006 103 12 4362 4365
    • (2006) Proc. Natl. Acad. Sci. U. S. A. , vol.103 , Issue.12 , pp. 4362-4365
    • Cohen, A.E.1    Moerner, W.E.2
  • 127
    • 84861007296 scopus 로고    scopus 로고
    • Microscopy beyond the diffraction limit using actively controlled single molecules
    • W. E. Moerner Microscopy beyond the diffraction limit using actively controlled single molecules J. Microsc. 2012 246 3 213 220
    • (2012) J. Microsc. , vol.246 , Issue.3 , pp. 213-220
    • Moerner, W.E.1
  • 128
    • 78149261019 scopus 로고    scopus 로고
    • Three-dimensional tracking of single mRNA particles in Saccharomyces cerevisiae using a double-helix point spread function
    • M. A. Thompson J. M. Casolari M. Badieirostami P. O. Brown W. E. Moerner Three-dimensional tracking of single mRNA particles in Saccharomyces cerevisiae using a double-helix point spread function Proc. Natl. Acad. Sci. U. S. A. 2010 107 42 17864 17871
    • (2010) Proc. Natl. Acad. Sci. U. S. A. , vol.107 , Issue.42 , pp. 17864-17871
    • Thompson, M.A.1    Casolari, J.M.2    Badieirostami, M.3    Brown, P.O.4    Moerner, W.E.5
  • 129
    • 84869853938 scopus 로고    scopus 로고
    • Probing Single Biomolecules in Solution Using the Anti-Brownian Electrokinetic (ABEL) Trap
    • Q. Wang R. H. Goldsmith Y. Jiang S. D. Bockenhauer W. E. Moerner Probing Single Biomolecules in Solution Using the Anti-Brownian Electrokinetic (ABEL) Trap Acc. Chem. Res. 2012 45 11 1955 1964
    • (2012) Acc. Chem. Res. , vol.45 , Issue.11 , pp. 1955-1964
    • Wang, Q.1    Goldsmith, R.H.2    Jiang, Y.3    Bockenhauer, S.D.4    Moerner, W.E.5
  • 130
    • 34548098881 scopus 로고    scopus 로고
    • Super- and sub-Poissonian photon statistics for single molecule spectroscopy
    • Y. He E. Barkai Super- and sub-Poissonian photon statistics for single molecule spectroscopy J. Chem. Phys. 2005 122 18 184703
    • (2005) J. Chem. Phys. , vol.122 , Issue.18 , pp. 184703
    • He, Y.1    Barkai, E.2
  • 131
    • 41849107614 scopus 로고    scopus 로고
    • Single molecule conformational dynamics of adenylate kinase: Energy landscape, structural correlations, and transition state ensembles
    • DOI 10.1021/ja0780481
    • Q. Lu J. Wang Single molecule conformational dynamics of adenylate kinase: Energy landscape, structural correlations, and transition state ensembles J. Am. Chem. Soc. 2008 130 14 4772 4783 (Pubitemid 351500112)
    • (2008) Journal of the American Chemical Society , vol.130 , Issue.14 , pp. 4772-4783
    • Lu, Q.1    Wang, J.2
  • 132
    • 33748096830 scopus 로고    scopus 로고
    • Open-system nonequilibrium steady state: Statistical thermodynamics, fluctuations, and chemical oscillations
    • DOI 10.1021/jp061858z
    • H. Qian Open-system nonequilibrium steady state: statistical thermodynamics, fluctuations, and chemical oscillations J. Phys. Chem. B 2006 110 31 15063 15074 (Pubitemid 44334760)
    • (2006) Journal of Physical Chemistry B , vol.110 , Issue.31 , pp. 15063-15074
    • Qian, H.1
  • 133
    • 0037058951 scopus 로고    scopus 로고
    • Single-molecule enzymology: Stochastic Michaelis-Menten kinetics
    • DOI 10.1016/S0301-4622(02)00145-X, PII S030146220200145X
    • H. Qian E. L. Elson Single-molecule enzymology: stochastic Michaelis-Menten kinetics Biophys. Chem. 2002 101 565 576 (Pubitemid 35462072)
    • (2002) Biophysical Chemistry , vol.101-102 , pp. 565-576
    • Qian, H.1    Elson, E.L.2
  • 136
    • 0037461523 scopus 로고    scopus 로고
    • Direct measurements of memory effects in single-molecule kinetics
    • S. L. Yang J. S. Cao Direct measurements of memory effects in single-molecule kinetics J. Chem. Phys. 2002 117 24 10996 11009
    • (2002) J. Chem. Phys. , vol.117 , Issue.24 , pp. 10996-11009
    • Yang, S.L.1    Cao, J.S.2
  • 137
    • 4344683522 scopus 로고    scopus 로고
    • Single molecule photon emission statistics for non-Markovian blinking models
    • Y. J. Zheng F. L. H. Brown Single molecule photon emission statistics for non-Markovian blinking models J. Chem. Phys. 2004 121 7 3238 3252
    • (2004) J. Chem. Phys. , vol.121 , Issue.7 , pp. 3238-3252
    • Zheng, Y.J.1    Brown, F.L.H.2
  • 138
    • 73649092707 scopus 로고    scopus 로고
    • Single-Molecule Study of DNA Polymerization Activity of HIV-1 Reverse Transcriptase on DNA Templates
    • S. Kim C. M. Schroeder X. S. Xie Single-Molecule Study of DNA Polymerization Activity of HIV-1 Reverse Transcriptase on DNA Templates J. Mol. Biol. 2010 395 5 995 1006
    • (2010) J. Mol. Biol. , vol.395 , Issue.5 , pp. 995-1006
    • Kim, S.1    Schroeder, C.M.2    Xie, X.S.3
  • 139
    • 39249085041 scopus 로고    scopus 로고
    • Time-dependent fluctuations in single molecule spectroscopy: A generalized Wiener-Khintchine approach
    • E. Barkai Y. Jung R. Silbey Time-dependent fluctuations in single molecule spectroscopy: a generalized Wiener-Khintchine approach Phys. Rev. Lett. 2001 87 20 207403
    • (2001) Phys. Rev. Lett. , vol.87 , Issue.20 , pp. 207403
    • Barkai, E.1    Jung, Y.2    Silbey, R.3
  • 140
    • 0034299428 scopus 로고    scopus 로고
    • Transition from simple to complex behavior of single molecule line shapes in disordered condensed phase
    • E. Barkai R. Silbey G. Zumofen Transition from simple to complex behavior of single molecule line shapes in disordered condensed phase J. Chem. Phys. 2000 113 14 5853 5867
    • (2000) J. Chem. Phys. , vol.113 , Issue.14 , pp. 5853-5867
    • Barkai, E.1    Silbey, R.2    Zumofen, G.3
  • 141
    • 45849095234 scopus 로고    scopus 로고
    • How do proteins interact?
    • DOI 10.1126/science.1158818
    • D. D. Boehr P. E. Wright How do proteins interact? Science 2008 320 5882 1429 1430 (Pubitemid 351929416)
    • (2008) Science , vol.320 , Issue.5882 , pp. 1429-1430
    • Boehr, D.D.1    Wright, P.E.2
  • 142
    • 0037449908 scopus 로고    scopus 로고
    • Single-molecule kinetics with time-dependent rates: A generating function approach
    • F. L. H. Brown Single-molecule kinetics with time-dependent rates: a generating function approach Phys. Rev. Lett. 2003 90 2 028302
    • (2003) Phys. Rev. Lett. , vol.90 , Issue.2 , pp. 028302
    • Brown, F.L.H.1
  • 143
    • 84962422584 scopus 로고    scopus 로고
    • Catalysis and specificity in enzymes: A study of triosephosphate isomerase and comparison with methyl glyoxal synthase
    • DOI 10.1016/S0065-3233(03)66008-0
    • Q. Cui M. Karplus Catalysis and specificity in enzymes: a study of triosephosphate isomerase and comparison with methyl glyoxal synthase Adv. Protein Chem. 2003 66 315 372 (Pubitemid 37392319)
    • (2003) Advances in Protein Chemistry , vol.66 , pp. 315-372
    • Cui, Q.1    Karplus, M.2
  • 144
    • 4243155782 scopus 로고    scopus 로고
    • NMR characterization of the dynamics of biomacromolecules
    • A. G. Palmer NMR characterization of the dynamics of biomacromolecules Chem. Rev. 2004 104 8 3623 3640
    • (2004) Chem. Rev. , vol.104 , Issue.8 , pp. 3623-3640
    • Palmer, A.G.1
  • 147
    • 7044247472 scopus 로고    scopus 로고
    • Probing nanosecond protein motions of calmodulin by single-molecule fluorescence anisotropy
    • X. Tan D. H. Hu T. C. Squier H. P. Lu Probing nanosecond protein motions of calmodulin by single-molecule fluorescence anisotropy Appl. Phys. Lett. 2004 85 12 2420 2422
    • (2004) Appl. Phys. Lett. , vol.85 , Issue.12 , pp. 2420-2422
    • Tan, X.1    Hu, D.H.2    Squier, T.C.3    Lu, H.P.4
  • 149
    • 0032503999 scopus 로고    scopus 로고
    • Specific covalent labeling of recombinant protein molecules inside live cells
    • DOI 10.1126/science.281.5374.269
    • B. A. Griffin S. R. Adams R. Y. Tsien Specific covalent labeling of recombinant protein molecules inside live cells Science 1998 281 5374 269 272 (Pubitemid 28334512)
    • (1998) Science , vol.281 , Issue.5374 , pp. 269-272
    • Griffin, B.A.1    Adams, S.R.2    Tsien, R.Y.3
  • 150
    • 79551525710 scopus 로고    scopus 로고
    • Five challenges to bringing single-molecule force spectroscopy into living cells
    • Y. F. Dufrene et al., Five challenges to bringing single-molecule force spectroscopy into living cells Nat. Methods 2011 8 2 123 127
    • (2011) Nat. Methods , vol.8 , Issue.2 , pp. 123-127
    • Dufrene, Y.F.1
  • 151
    • 84877785401 scopus 로고    scopus 로고
    • Nanoapertures for AFM-based single-molecule force spectroscopy
    • S. F. Heucke et al., Nanoapertures for AFM-based single-molecule force spectroscopy Int. J. Nanotechnol. 2013 10 5-7 607 619
    • (2013) Int. J. Nanotechnol. , vol.10 , Issue.57 , pp. 607-619
    • Heucke, S.F.1
  • 152
    • 78650212529 scopus 로고    scopus 로고
    • Mechanoenzymatics and Nanoassembly of Single Molecules
    • ed. A. Graslund, R. Rigler and J. Widengren
    • E. M. Puchner and H. E. Gaub, Mechanoenzymatics and Nanoassembly of Single Molecules, in Single Molecule Spectroscopy in Chemistry, Physics and Biology, ed., A. Graslund, R. Rigler, and, J. Widengren, 2010, vol. 96, pp. 289-303
    • (2010) Single Molecule Spectroscopy in Chemistry, Physics and Biology , vol.96 , pp. 289-303
    • Puchner, E.M.1    Gaub, H.E.2
  • 153
    • 84866503266 scopus 로고    scopus 로고
    • Nanoscale Arrangement of Proteins by Single-Molecule Cut-and-Paste
    • M. Strackharn D. A. Pippig P. Meyer S. W. Stahl H. E. Gaub Nanoscale Arrangement of Proteins by Single-Molecule Cut-and-Paste J. Am. Chem. Soc. 2012 134 37 15193 15196
    • (2012) J. Am. Chem. Soc. , vol.134 , Issue.37 , pp. 15193-15196
    • Strackharn, M.1    Pippig, D.A.2    Meyer, P.3    Stahl, S.W.4    Gaub, H.E.5
  • 154
    • 79955640296 scopus 로고    scopus 로고
    • Single-molecule paleoenzymology probes the chemistry of resurrected enzymes
    • R. Perez-Jimenez et al., Single-molecule paleoenzymology probes the chemistry of resurrected enzymes Nat. Struct. Mol. Biol. 2011 18 5 592 596
    • (2011) Nat. Struct. Mol. Biol. , vol.18 , Issue.5 , pp. 592-596
    • Perez-Jimenez, R.1
  • 155
    • 84859190303 scopus 로고    scopus 로고
    • Total internal reflection fluorescence microscopy imaging-guided confocal single-molecule fluorescence spectroscopy
    • D. S. Zheng L. Kaldaras H. P. Lu Total internal reflection fluorescence microscopy imaging-guided confocal single-molecule fluorescence spectroscopy Rev. Sci. Instrum. 2012 83 1 013110
    • (2012) Rev. Sci. Instrum. , vol.83 , Issue.1 , pp. 013110
    • Zheng, D.S.1    Kaldaras, L.2    Lu, H.P.3
  • 156
    • 0031127502 scopus 로고    scopus 로고
    • Protein hinge bending as seen in molecular dynamics simulations of native and M6I mutant T4 lysozymes
    • G. E. Arnold R. L. Ornstein Protein hinge bending as seen in molecular dynamics simulations of native and M6I mutant T4 lysozymes Biopolymers 1997 41 5 533 544
    • (1997) Biopolymers , vol.41 , Issue.5 , pp. 533-544
    • Arnold, G.E.1    Ornstein, R.L.2
  • 158
    • 79955447968 scopus 로고    scopus 로고
    • Michaelis-Menten Equation and Detailed Balance in Enzymatic Networks
    • J. Cao Michaelis-Menten Equation and Detailed Balance in Enzymatic Networks J. Phys. Chem. B 2011 115 18 5493 5498
    • (2011) J. Phys. Chem. B , vol.115 , Issue.18 , pp. 5493-5498
    • Cao, J.1
  • 159
    • 0003028926 scopus 로고    scopus 로고
    • Event-averaged measurements of single-molecule kinetics
    • J. S. Cao Event-averaged measurements of single-molecule kinetics Chem. Phys. Lett. 2000 327 1-2 38 44
    • (2000) Chem. Phys. Lett. , vol.327 , Issue.12 , pp. 38-44
    • Cao, J.S.1
  • 160
    • 79958223719 scopus 로고    scopus 로고
    • Excitation Energy Transfer in a Non-Markovian Dynamical Disordered Environment: Localization, Narrowing, and Transfer Efficiency
    • X. Chen R. J. Silbey Excitation Energy Transfer in a Non-Markovian Dynamical Disordered Environment: Localization, Narrowing, and Transfer Efficiency J. Phys. Chem. B 2011 115 18 5499 5509
    • (2011) J. Phys. Chem. B , vol.115 , Issue.18 , pp. 5499-5509
    • Chen, X.1    Silbey, R.J.2
  • 161
    • 22244469413 scopus 로고    scopus 로고
    • What can one learn from two-state single-molecule trajectories?
    • DOI 10.1529/biophysj.104.055905
    • O. Flomenbom J. Klafter A. Szabo What can one learn from two-state single-molecule trajectories? Biophys. J. 2005 88 6 3780 3783 (Pubitemid 40991093)
    • (2005) Biophysical Journal , vol.88 , Issue.6 , pp. 3780-3783
    • Flomenbom, O.1    Klafter, J.2    Szabo, A.3
  • 162
    • 77953064853 scopus 로고    scopus 로고
    • Effect of correlation of local fluctuations on exciton coherence
    • X. Chen R. J. Silbey Effect of correlation of local fluctuations on exciton coherence J. Chem. Phys. 2010 132 20 204503
    • (2010) J. Chem. Phys. , vol.132 , Issue.20 , pp. 204503
    • Chen, X.1    Silbey, R.J.2
  • 163
    • 36048957951 scopus 로고    scopus 로고
    • An interpretation of fluctuations in enzyme catalysis rate, spectral diffusion, and radiative component of lifetimes in terms of electric field fluctuations
    • DOI 10.1073/pnas.0707859104
    • M. K. Prakash R. A. Marcus An interpretation of fluctuations in enzyme catalysis rate, spectral diffusion, and radiative component of lifetimes in terms of electric field fluctuations Proc. Natl. Acad. Sci. U. S. A. 2007 104 41 15982 15987 (Pubitemid 350099345)
    • (2007) Proceedings of the National Academy of Sciences of the United States of America , vol.104 , Issue.41 , pp. 15982-15987
    • Prakash, M.K.1    Marcus, R.A.2
  • 164
    • 4644236471 scopus 로고    scopus 로고
    • Hydrophobic collapse in multidomain protein folding
    • DOI 10.1126/science.1101176
    • R. H. Zhou X. H. Huang C. J. Margulis B. J. Berne Hydrophobic collapse in multidomain protein folding Science 2004 305 5690 1605 1609 (Pubitemid 39296352)
    • (2004) Science , vol.305 , Issue.5690 , pp. 1605-1609
    • Zhou, R.1    Huang, X.2    Margulis, C.J.3    Berne, B.J.4
  • 165
    • 69549120472 scopus 로고    scopus 로고
    • Conformational selection or induced fit: A flux description of reaction mechanism
    • G. G. Hammes Y.-C. Chang T. G. Oas Conformational selection or induced fit: a flux description of reaction mechanism Proc. Natl. Acad. Sci. U. S. A. 2009 106 33 13737 13741
    • (2009) Proc. Natl. Acad. Sci. U. S. A. , vol.106 , Issue.33 , pp. 13737-13741
    • Hammes, G.G.1    Chang, Y.-C.2    Oas, T.G.3
  • 166
    • 52949089027 scopus 로고    scopus 로고
    • Enzymes with lid-gated active sites must operate by an induced fit mechanism instead of conformational selection
    • S. M. Sullivan T. Holyoak Enzymes with lid-gated active sites must operate by an induced fit mechanism instead of conformational selection Proc. Natl. Acad. Sci. U. S. A. 2008 105 37 13829 13834
    • (2008) Proc. Natl. Acad. Sci. U. S. A. , vol.105 , Issue.37 , pp. 13829-13834
    • Sullivan, S.M.1    Holyoak, T.2
  • 167
    • 73349117207 scopus 로고    scopus 로고
    • Conformational selection and induced fit mechanism underlie specificity in noncovalent interactions with ubiquitin
    • T. Wlodarski B. Zagrovic Conformational selection and induced fit mechanism underlie specificity in noncovalent interactions with ubiquitin Proc. Natl. Acad. Sci. U. S. A. 2009 106 46 19346 19351
    • (2009) Proc. Natl. Acad. Sci. U. S. A. , vol.106 , Issue.46 , pp. 19346-19351
    • Wlodarski, T.1    Zagrovic, B.2
  • 169
    • 79952745560 scopus 로고    scopus 로고
    • Role of large thermal fluctuations and magnesium ions in t-RNA selectivity of the ribosome
    • Z. J. Guo M. Gibson S. Sitha S. Chu U. Mohanty Role of large thermal fluctuations and magnesium ions in t-RNA selectivity of the ribosome Proc. Natl. Acad. Sci. U. S. A. 2011 108 10 3947 3951
    • (2011) Proc. Natl. Acad. Sci. U. S. A. , vol.108 , Issue.10 , pp. 3947-3951
    • Guo, Z.J.1    Gibson, M.2    Sitha, S.3    Chu, S.4    Mohanty, U.5
  • 170
    • 77954900239 scopus 로고    scopus 로고
    • Substrate-induced Changes in Protease Active Site Conformation Impact on Subsequent Reactions with Substrates
    • R. Pan et al., Substrate-induced Changes in Protease Active Site Conformation Impact on Subsequent Reactions with Substrates J. Biol. Chem. 2010 285 30 22948 22954
    • (2010) J. Biol. Chem. , vol.285 , Issue.30 , pp. 22948-22954
    • Pan, R.1
  • 171
    • 37549017736 scopus 로고    scopus 로고
    • Visualizing spatially correlated dynamics that directs RNA conformational transitions
    • Q. Zhang A. C. Stelzer C. K. Fisher H. M. Al-Hashimi Visualizing spatially correlated dynamics that directs RNA conformational transitions Nature 2007 450 7173 1263 1267
    • (2007) Nature , vol.450 , Issue.7173 , pp. 1263-1267
    • Zhang, Q.1    Stelzer, A.C.2    Fisher, C.K.3    Al-Hashimi, H.M.4
  • 172
    • 0027130476 scopus 로고
    • Imposed oscillations of kinetic barriers can cause an enzyme to drive a chemical reaction away from equilibrium
    • R. D. Astumian B. Robertson Imposed Oscillations of Kinetic Barriers Can Cause an Enzyme to Drive a Chemical Reaction Away from Equilibrium J. Am. Chem. Soc. 1993 115 24 11063 11068 (Pubitemid 2000303)
    • (1993) Journal of the American Chemical Society , vol.115 , Issue.24 , pp. 11063-11068
    • Astumian, R.D.1    Robertson, B.2
  • 173
    • 1042299975 scopus 로고    scopus 로고
    • Essential Roles of a Dynamic Loop in the Catalysis of 6-Hydroxymethyl-7,8-dihydropterin Pyrophosphokinase
    • DOI 10.1021/bi036053l
    • J. Blaszczyk et al., Essential roles of a dynamic loop in the catalysis of 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase Biochemistry 2004 43 6 1469 1477 (Pubitemid 38200552)
    • (2004) Biochemistry , vol.43 , Issue.6 , pp. 1469-1477
    • Blaszczyk, J.1    Li, Y.2    Wu, Y.3    Shi, G.4    Ji, X.5    Yan, H.6
  • 174
    • 1542476995 scopus 로고    scopus 로고
    • Reaction trajectory of pyrophosphoryl transfer catalyzed by 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase
    • DOI 10.1016/j.str.2004.02.003, PII S0969212604000450
    • J. Blaszczyk G. B. Shi Y. Li H. G. Yan X. H. Ji Reaction trajectory of pyrophosphoryl transfer catalyzed by 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase Structure 2004 12 3 467 475 (Pubitemid 38353067)
    • (2004) Structure , vol.12 , Issue.3 , pp. 467-475
    • Blaszczyk, J.1    Shi, G.2    Li, Y.3    Yan, H.4    Ji, X.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.