메뉴 건너뛰기




Volumn 19, Issue 12, 2014, Pages 19407-19434

Shedding light on protein folding, structural and functional dynamics by single molecule studies

Author keywords

Allosteric regulation; Conformational dynamics; Free energy landscape; Protein folding; Single molecule FRET; Single molecules

Indexed keywords

PROTEIN;

EID: 84919756005     PISSN: None     EISSN: 14203049     Source Type: Journal    
DOI: 10.3390/molecules191219407     Document Type: Review
Times cited : (16)

References (206)
  • 1
    • 33646937406 scopus 로고    scopus 로고
    • Single-molecule fluorescence studies of protein folding and conformational dynamics
    • Michalet, X.; Weiss, S.; Jager, M. Single-molecule fluorescence studies of protein folding and conformational dynamics. Chem. Rev. 2006, 106, 1785-1813.
    • (2006) Chem. Rev. , vol.106 , pp. 1785-1813
    • Michalet, X.1    Weiss, S.2    Jager, M.3
  • 2
    • 84893129964 scopus 로고    scopus 로고
    • Insights in enzyme functional dynamics and activity regulation by single molecule studies
    • Jorgensen, S.K.; Hatzakis, N.S. Insights in enzyme functional dynamics and activity regulation by single molecule studies. Biophys. Rev. Lett. 2013, 8, 137-160.
    • (2013) Biophys. Rev. Lett. , vol.8 , pp. 137-160
    • Jorgensen, S.K.1    Hatzakis, N.S.2
  • 3
    • 34547878369 scopus 로고    scopus 로고
    • New directions in single-molecule imaging and analysis
    • Moerner, W.E. New directions in single-molecule imaging and analysis. Proc. Natl. Acad. Sci. USA 2007, 104, 12596-12602.
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 12596-12602
    • Moerner, W.E.1
  • 4
    • 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
  • 5
    • 39149087014 scopus 로고    scopus 로고
    • Protein folding studied by single-molecule FRET
    • Schuler, B.; Eaton, W.A. Protein folding studied by single-molecule FRET. Curr. Opin. Struct. Biol. 2008, 18, 16-26.
    • (2008) Curr. Opin. Struct. Biol. , vol.18 , pp. 16-26
    • Schuler, B.1    Eaton, W.A.2
  • 6
    • 50649121477 scopus 로고    scopus 로고
    • Advances in single-molecule fluorescence methods for molecular biology
    • Joo, C.; Balci, H.; Ishitsuka, Y.; Buranachai, C.; Ha, T. Advances in single-molecule fluorescence methods for molecular biology. Annu. Rev. Biochem. 2008, 77, 51-76.
    • (2008) Annu. Rev. Biochem. , vol.77 , pp. 51-76
    • Joo, C.1    Balci, H.2    Ishitsuka, Y.3    Buranachai, C.4    Ha, T.5
  • 7
    • 33947517676 scopus 로고    scopus 로고
    • A survey of single-molecule techniques in chemical biology
    • Cornish, P.V.; Ha, T. A survey of single-molecule techniques in chemical biology. ACS Chem. Biol. 2007, 2, 53-61.
    • (2007) ACS Chem. Biol. , vol.2 , pp. 53-61
    • Cornish, P.V.1    Ha, T.2
  • 8
    • 84893394173 scopus 로고    scopus 로고
    • Shedding light on protein folding landscapes by single-molecule fluorescence
    • Banerjee, P.R.; Deniz, A.A. Shedding light on protein folding landscapes by single-molecule fluorescence. Chem. Soc. Rev. 2014, 43, 1172-1188.
    • (2014) Chem. Soc. Rev. , vol.43 , pp. 1172-1188
    • Banerjee, P.R.1    Deniz, A.A.2
  • 9
    • 84894264010 scopus 로고    scopus 로고
    • Single molecule insights on conformational selection and induced fit mechanism
    • Hatzakis, N.S. Single molecule insights on conformational selection and induced fit mechanism. Biophys. Chem. 2014, 186, 46-54.
    • (2014) Biophys. Chem. , vol.186 , pp. 46-54
    • Hatzakis, N.S.1
  • 11
    • 0032484096 scopus 로고    scopus 로고
    • Single-molecule enzymatic dynamics
    • Lu, H.P.; Xun, L.Y.; Xie, X.S. Single-molecule enzymatic dynamics. Science 1998, 282, 1877-1882.
    • (1998) Science , vol.282 , pp. 1877-1882
    • Lu, H.P.1    Xun, L.Y.2    Xie, X.S.3
  • 12
    • 69949092035 scopus 로고    scopus 로고
    • Direct observation of the binding state of the kinesin head to the microtubule
    • Guydosh, N.R.; Block, S.M. Direct observation of the binding state of the kinesin head to the microtubule. Nature 2009, 461, 125-129.
    • (2009) Nature , vol.461 , pp. 125-129
    • Guydosh, N.R.1    Block, S.M.2
  • 13
    • 79957935490 scopus 로고    scopus 로고
    • Substrate-modulated gating dynamics in a na(+)-coupled neurotransmitter transporter homologue
    • Zhao, Y.F.; Terry, D.S.; Shi, L.; Quick, M.; Weinstein, H.; Blanchard, S.C.; Javitch, J.A. Substrate-modulated gating dynamics in a Na(+)-coupled neurotransmitter transporter homologue. Nature 2011, 474, 109-113.
    • (2011) Nature , vol.474 , pp. 109-113
    • Zhao, Y.F.1    Terry, D.S.2    Shi, L.3    Quick, M.4    Weinstein, H.5    Blanchard, S.C.6    Javitch, J.A.7
  • 14
    • 67349279395 scopus 로고    scopus 로고
    • Detection and trapping of intermediate states priming nicotinic receptor channel opening
    • Mukhtasimova, N.; Lee, W.Y.; Wang, H.L.; Sine, S.M. Detection and trapping of intermediate states priming nicotinic receptor channel opening. Nature 2009, 459, 451-454.
    • (2009) Nature , vol.459 , pp. 451-454
    • Mukhtasimova, N.1    Lee, W.Y.2    Wang, H.L.3    Sine, S.M.4
  • 15
    • 54249083606 scopus 로고    scopus 로고
    • A stochastic single-molecule event triggers phenotype switching of a bacterial cell
    • Choi, P.J.; Cai, L.; Frieda, K.; Xie, S. A stochastic single-molecule event triggers phenotype switching of a bacterial cell. Science 2008, 322, 442-446.
    • (2008) Science , vol.322 , pp. 442-446
    • Choi, P.J.1    Cai, L.2    Frieda, K.3    Xie, S.4
  • 16
  • 17
    • 84861887087 scopus 로고    scopus 로고
    • Single enzyme studies reveal the existence of discrete functional states for monomeric enzymes and how they are "selected" upon allosteric regulation
    • Hatzakis, N.S.; Wei, L.; Jorgensen, S.K.; Kunding, A.H.; Bolinger, P.Y.; Ehrlich, N.; Makarov, I.; Skjot, M.; Svendsen, A.; Hedegard, P.; et al. Single enzyme studies reveal the existence of discrete functional states for monomeric enzymes and how they are "selected" upon allosteric regulation. J. Am. Chem. Soc. 2012, 134, 9296-9302.
    • (2012) J. Am. Chem. Soc. , vol.134 , pp. 9296-9302
    • Hatzakis, N.S.1    Wei, L.2    Jorgensen, S.K.3    Kunding, A.H.4    Bolinger, P.Y.5    Ehrlich, N.6    Makarov, I.7    Skjot, M.8    Svendsen, A.9    Hedegard, P.10
  • 18
    • 42149136142 scopus 로고    scopus 로고
    • Distinct and long-lived activity states of single enzyme molecules
    • Rissin, D.M.; Gorris, H.H.; Walt, D.R. Distinct and long-lived activity states of single enzyme molecules. J. Am. Chem. Soc. 2008, 130, 5349-5353.
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 5349-5353
    • Rissin, D.M.1    Gorris, H.H.2    Walt, D.R.3
  • 21
    • 0033056708 scopus 로고    scopus 로고
    • Folding funnels, binding funnels, and protein function
    • Tsai, C.J.; Kumar, S.; Ma, B.Y.; Nussinov, R. Folding funnels, binding funnels, and protein function. Protein Sci. 1999, 8, 1181-1190.
    • (1999) Protein Sci. , vol.8 , pp. 1181-1190
    • Tsai, C.J.1    Kumar, S.2    Ma, B.Y.3    Nussinov, R.4
  • 24
    • 44449097780 scopus 로고    scopus 로고
    • Do-it-yourself guide: How to use the modern single-molecule toolkit
    • Walter, N.G.; Huang, C.Y.; Manzo, A.J.; Sobhy, M.A. Do-it-yourself guide: How to use the modern single-molecule toolkit. Nat. Methods 2008, 5, 475-489.
    • (2008) Nat. Methods , vol.5 , pp. 475-489
    • Walter, N.G.1    Huang, C.Y.2    Manzo, A.J.3    Sobhy, M.A.4
  • 25
    • 84890456968 scopus 로고    scopus 로고
    • Maximizing information content of single-molecule FRET experiments: Multi-color FRET and FRET combined with force or torque
    • Hohng, S.; Lee, S.; Lee, J.; Jo, M.H. Maximizing information content of single-molecule FRET experiments: multi-color FRET and FRET combined with force or torque. Chem. Soc. Rev. 2014, 43, 1007-1013.
    • (2014) Chem. Soc. Rev. , vol.43 , pp. 1007-1013
    • Hohng, S.1    Lee, S.2    Lee, J.3    Jo, M.H.4
  • 26
    • 44449087047 scopus 로고    scopus 로고
    • Single-molecule force spectroscopy: Optical tweezers, magnetic tweezers and atomic force microscopy
    • Neuman, K.C.; Nagy, A. Single-molecule force spectroscopy: Optical tweezers, magnetic tweezers and atomic force microscopy. Nat. Methods 2008, 5, 491-505.
    • (2008) Nat. Methods , vol.5 , pp. 491-505
    • Neuman, K.C.1    Nagy, A.2
  • 27
    • 84867657357 scopus 로고    scopus 로고
    • Force probing of individual molecules inside the living cell is now a reality
    • Oddershede, L.B. Force probing of individual molecules inside the living cell is now a reality. Nat. Chem. Biol. 2012, 8, 879-886.
    • (2012) Nat. Chem. Biol. , vol.8 , pp. 879-886
    • Oddershede, L.B.1
  • 29
    • 79957848754 scopus 로고    scopus 로고
    • Optical tweezers study life under tension
    • Fazal, F.M.; Block, S.M. Optical tweezers study life under tension. Nat. Photonics 2011, 5, 318-321.
    • (2011) Nat. Photonics , vol.5 , pp. 318-321
    • Fazal, F.M.1    Block, S.M.2
  • 30
    • 0343777458 scopus 로고    scopus 로고
    • Observing single biomolecules at work with the atomic force microscope
    • Engel, A.; Muller, D.J. Observing single biomolecules at work with the atomic force microscope. Nat. Struct. Biol. 2000, 7, 715-718.
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 715-718
    • Engel, A.1    Muller, D.J.2
  • 31
    • 0033817704 scopus 로고    scopus 로고
    • Stretching single molecules into novel conformations using the atomic force microscope
    • Fisher, T.E.; Marszalek, P.E.; Fernandez, J.M. Stretching single molecules into novel conformations using the atomic force microscope. Nat. Struct. Biol. 2000, 7, 719-724.
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 719-724
    • Fisher, T.E.1    Marszalek, P.E.2    Fernandez, J.M.3
  • 32
    • 49649113590 scopus 로고    scopus 로고
    • Towards nanomicrobiology using atomic force microscopy
    • Dufrene, Y.F. Towards nanomicrobiology using atomic force microscopy. Nat. Rev. Microbiol. 2008, 6, 674-680.
    • (2008) Nat. Rev. Microbiol. , vol.6 , pp. 674-680
    • Dufrene, Y.F.1
  • 33
    • 43449133266 scopus 로고    scopus 로고
    • Atomic force microscopy as a multifunctional molecular toolbox in nanobiotechnology
    • Muller, D.J.; Dufrene, Y.F. Atomic force microscopy as a multifunctional molecular toolbox in nanobiotechnology. Nat. Nanotech. 2008, 3, 261-269.
    • (2008) Nat. Nanotech. , vol.3 , pp. 261-269
    • Muller, D.J.1    Dufrene, Y.F.2
  • 34
    • 65949083762 scopus 로고    scopus 로고
    • Force probing surfaces of living cells to molecular resolution
    • Muller, D.J.; Helenius, J.; Alsteens, D.; Dufrene, Y.F. Force probing surfaces of living cells to molecular resolution. Nat. Chem. Biol. 2009, 5, 383-390.
    • (2009) Nat. Chem. Biol. , vol.5 , pp. 383-390
    • Muller, D.J.1    Helenius, J.2    Alsteens, D.3    Dufrene, Y.F.4
  • 35
    • 77951643876 scopus 로고    scopus 로고
    • Probing cellular events, one quantum dot at a time
    • Pinaud, F.; Clarke, S.; Sittner, A.; Dahan, M. Probing cellular events, one quantum dot at a time. Nat. Methods 2010, 7, 275-285.
    • (2010) Nat. Methods , vol.7 , pp. 275-285
    • Pinaud, F.1    Clarke, S.2    Sittner, A.3    Dahan, M.4
  • 36
    • 75149125135 scopus 로고    scopus 로고
    • Progress in single-molecule spectroscopy in cells
    • Yang, H. Progress in single-molecule spectroscopy in cells. Curr. Opin. Chem. Biol. 2010, 14, 3-9.
    • (2010) Curr. Opin. Chem. Biol. , vol.14 , pp. 3-9
    • Yang, H.1
  • 37
    • 79951971261 scopus 로고    scopus 로고
    • Moving into the cell: Single-molecule studies of molecular motors in complex environments
    • Veigel, C.; Schmidt, C.F. Moving into the cell: Single-molecule studies of molecular motors in complex environments. Nat. Rev. Mol. Cell Bio. 2011, 12, 163-176.
    • (2011) Nat. Rev. Mol. Cell Bio. , vol.12 , pp. 163-176
    • Veigel, C.1    Schmidt, C.F.2
  • 38
    • 84861374075 scopus 로고    scopus 로고
    • Single-molecule views of protein movement on single-stranded DNA
    • Ha, T.; Kozlov, A.G.; Lohman, T.M. Single-molecule views of protein movement on single-stranded DNA. Annu. Rev. Biophys. 2012, 41, 295-319.
    • (2012) Annu. Rev. Biophys. , vol.41 , pp. 295-319
    • Ha, T.1    Kozlov, A.G.2    Lohman, T.M.3
  • 40
    • 33748614065 scopus 로고    scopus 로고
    • Single molecule studies of enzyme mechanisms
    • Smiley, R.D.; Hammes, G.G. Single molecule studies of enzyme mechanisms. Chem. Rev. 2006, 106, 3080-3094.
    • (2006) Chem. Rev. , vol.106 , pp. 3080-3094
    • Smiley, R.D.1    Hammes, G.G.2
  • 42
    • 18844423055 scopus 로고    scopus 로고
    • Branching out of single-molecule fluorescence spectroscopy: Challenges for chemistry and influence on biology
    • Tinnefeld, P.; Sauer, M. Branching out of single-molecule fluorescence spectroscopy: Challenges for chemistry and influence on biology. Angew. Chem. Int. Ed. 2005, 44, 2642-2671.
    • (2005) Angew. Chem. Int. Ed. , vol.44 , pp. 2642-2671
    • Tinnefeld, P.1    Sauer, M.2
  • 45
    • 84886954019 scopus 로고    scopus 로고
    • Single-molecule fluorescence probes dynamics of barrier crossing
    • Chung, H.S.; Eaton, W.A. Single-molecule fluorescence probes dynamics of barrier crossing. Nature 2013, 502, 685-688.
    • (2013) Nature , vol.502 , pp. 685-688
    • Chung, H.S.1    Eaton, W.A.2
  • 47
    • 34547877610 scopus 로고    scopus 로고
    • Fueling protein-DNA interactions inside porous nanocontainers
    • Cisse, I.; Okumus, B.; Joo, C.; Ha, T. Fueling protein-DNA interactions inside porous nanocontainers. Proc. Natl. Acad. Sci. USA 2007, 104, 12646-12650.
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 12646-12650
    • Cisse, I.1    Okumus, B.2    Joo, C.3    Ha, T.4
  • 49
    • 83655164333 scopus 로고    scopus 로고
    • Detecting intramolecular conformational dynamics of single molecules in short distance range with subnanometer sensitivity
    • Zhou, R.B.; Kunzelmann, S.; Webb, M.R.; Ha, T. Detecting intramolecular conformational dynamics of single molecules in short distance range with subnanometer sensitivity. Nano Lett. 2011, 11, 5482-5488.
    • (2011) Nano Lett. , vol.11 , pp. 5482-5488
    • Zhou, R.B.1    Kunzelmann, S.2    Webb, M.R.3    Ha, T.4
  • 50
    • 0015859467 scopus 로고
    • Principles that govern the folding of protein chains
    • Anfinsen, C.B. Principles that govern the folding of protein chains. Science 1973, 181, 223-230.
    • (1973) Science , vol.181 , pp. 223-230
    • Anfinsen, C.B.1
  • 51
    • 0023449962 scopus 로고
    • Spin-glasses and the statistical-mechanics of protein folding
    • Bryngelson, J.D.; Wolynes, P.G. Spin-glasses and the statistical-mechanics of protein folding. Proc. Natl. Acad. Sci. USA 1987, 84, 7524-7528.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 7524-7528
    • Bryngelson, J.D.1    Wolynes, P.G.2
  • 52
    • 79959385914 scopus 로고    scopus 로고
    • Behind the folding funnel diagram
    • Karplus, M. Behind the folding funnel diagram. Nat. Chem. Biol. 2011, 7, 401-404.
    • (2011) Nat. Chem. Biol. , vol.7 , pp. 401-404
    • Karplus, M.1
  • 54
    • 0014364651 scopus 로고
    • Protein denaturation
    • Tanford, C. Protein denaturation. Adv. Protein Chem. 1968, 23, 121-282.
    • (1968) Adv. Protein Chem. , vol.23 , pp. 121-282
    • Tanford, C.1
  • 55
    • 0020024242 scopus 로고
    • Specific intermediates in the folding reactions of small proteins and the mechanism of protein folding
    • Kim, P.S.; Baldwin, R.L. Specific intermediates in the folding reactions of small proteins and the mechanism of protein folding. Annu. Rev. Biochem. 1982, 51, 459-489.
    • (1982) Annu. Rev. Biochem. , vol.51 , pp. 459-489
    • Kim, P.S.1    Baldwin, R.L.2
  • 56
    • 0026320866 scopus 로고
    • The energy landscapes and motions of proteins
    • Frauenfelder, H.; Sligar, S.G.; Wolynes, P.G. The energy landscapes and motions of proteins. Science 1991, 254, 1598-1603.
    • (1991) Science , vol.254 , pp. 1598-1603
    • Frauenfelder, H.1    Sligar, S.G.2    Wolynes, P.G.3
  • 57
    • 33747065536 scopus 로고    scopus 로고
    • Multiple-basin energy landscapes for large-amplitude conformational motions of proteins: Structure-based molecular dynamics simulations
    • Okazaki, K.; Koga, N.; Takada, S.; Onuchic, J.N.; Wolynes, P.G. Multiple-basin energy landscapes for large-amplitude conformational motions of proteins: Structure-based molecular dynamics simulations. Proc. Natl. Acad. Sci. USA 2006, 103, 11844-11849.
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 11844-11849
    • Okazaki, K.1    Koga, N.2    Takada, S.3    Onuchic, J.N.4    Wolynes, P.G.5
  • 58
    • 0028947257 scopus 로고
    • Funnels, pathways, and the energy landscape of protein folding: A synthesis
    • Bryngelson, J.D.; Onuchic, J.N.; Socci, N.D.; Wolynes, P.G. Funnels, pathways, and the energy landscape of protein folding: A synthesis. Proteins 1995, 21, 167-195.
    • (1995) Proteins , vol.21 , pp. 167-195
    • Bryngelson, J.D.1    Onuchic, J.N.2    Socci, N.D.3    Wolynes, P.G.4
  • 59
    • 1842298212 scopus 로고    scopus 로고
    • From levinthal to pathways to funnels
    • Dill, K.A.; Chan, H.S. From Levinthal to pathways to funnels. Nat. Struct. Biol. 1997, 4, 10-19.
    • (1997) Nat. Struct. Biol. , vol.4 , pp. 10-19
    • Dill, K.A.1    Chan, H.S.2
  • 60
    • 84893372728 scopus 로고    scopus 로고
    • Sizing up single-molecule enzymatic conformational dynamics
    • Lu, H.P. Sizing up single-molecule enzymatic conformational dynamics. Chem. Soc. Rev. 2014, 43, 1118-1143.
    • (2014) Chem. Soc. Rev. , vol.43 , pp. 1118-1143
    • Lu, H.P.1
  • 61
    • 84873527015 scopus 로고    scopus 로고
    • Single-molecule spectroscopy of protein folding dynamics-expanding scope and timescales
    • Schuler, B.; Hofmann, H. Single-molecule spectroscopy of protein folding dynamics-Expanding scope and timescales. Curr. Opin. Struct. Biol. 2013, 23, 36-47.
    • (2013) Curr. Opin. Struct. Biol. , vol.23 , pp. 36-47
    • Schuler, B.1    Hofmann, H.2
  • 62
    • 84901272377 scopus 로고    scopus 로고
    • Studies of protein folding and dynamics using single molecule fluorescence spectroscopy
    • Basak, S.; Chattopadhyay, K. Studies of protein folding and dynamics using single molecule fluorescence spectroscopy. Phys. Chem. Chem. Phys. 2014, 16, 11139-11149.
    • (2014) Phys. Chem. Chem. Phys. , vol.16 , pp. 11139-11149
    • Basak, S.1    Chattopadhyay, K.2
  • 65
    • 0037126290 scopus 로고    scopus 로고
    • Probing the free-energy surface for protein folding with single-molecule fluorescence spectroscopy
    • Schuler, B.; Lipman, E.A.; Eaton, W.A. Probing the free-energy surface for protein folding with single-molecule fluorescence spectroscopy. Nature 2002, 419, 743-747.
    • (2002) Nature , vol.419 , pp. 743-747
    • Schuler, B.1    Lipman, E.A.2    Eaton, W.A.3
  • 66
    • 1842607369 scopus 로고    scopus 로고
    • Biofunctionalized, ultrathin coatings of cross-linked star-shaped poly(ethylene oxide) allow reversible folding of immobilized proteins
    • Groll, J.; Amirgoulova, E.V.; Ameringer, T.; Heyes, C.D.; Rocker, C.; Nienhaus, G.U.; Moller, M. Biofunctionalized, ultrathin coatings of cross-linked star-shaped poly(ethylene oxide) allow reversible folding of immobilized proteins. J. Am. Chem. Soc. 2004, 126, 4234-4239.
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 4234-4239
    • Groll, J.1    Amirgoulova, E.V.2    Ameringer, T.3    Heyes, C.D.4    Rocker, C.5    Nienhaus, G.U.6    Moller, M.7
  • 67
    • 84886644051 scopus 로고    scopus 로고
    • Gradual disordering of the native state on a slow two-state folding protein monitored by single-molecule fluorescence spectroscopy and NMR
    • Campos, L.A.; Sadqi, M.; Liu, J.; Wang, X.; English, D.S.; Muñoz, V. Gradual disordering of the native state on a slow two-state folding protein monitored by single-molecule fluorescence spectroscopy and NMR. J. Phys. Chem. B 2013, 117, 13120-13131.
    • (2013) J. Phys. Chem. B , vol.117 , pp. 13120-13131
    • Campos, L.A.1    Sadqi, M.2    Liu, J.3    Wang, X.4    English, D.S.5    Muñoz, V.6
  • 68
    • 0041321045 scopus 로고    scopus 로고
    • Single-molecule measurement of protein folding kinetics
    • Lipman, E.A.; Schuler, B.; Bakajin, O.; Eaton, W.A. Single-molecule measurement of protein folding kinetics. Science 2003, 301, 1233-1235.
    • (2003) Science , vol.301 , pp. 1233-1235
    • Lipman, E.A.1    Schuler, B.2    Bakajin, O.3    Eaton, W.A.4
  • 69
    • 0035811052 scopus 로고    scopus 로고
    • Lifetimes of intermediates in the beta-sheet to alpha-helix transition of beta-lactoglobulin by using a diffusional IR mixer
    • Kauffmann, E.; Darnton, N.C.; Austin, R.H.; Batt, C.; Gerwert, K. Lifetimes of intermediates in the beta-sheet to alpha-helix transition of beta-lactoglobulin by using a diffusional IR mixer. Proc. Natl. Acad. Sci. USA 2001, 98, 6646-6649.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 6646-6649
    • Kauffmann, E.1    Darnton, N.C.2    Austin, R.H.3    Batt, C.4    Gerwert, K.5
  • 70
    • 84880295113 scopus 로고    scopus 로고
    • Microfluidic mixer designed for performing single-molecule kinetics with confocal detection on timescales from milliseconds to minutes
    • Wunderlich, B.; Nettels, D.; Benke, S.; Clark, J.; Weidner, S.; Hofmann, H.; Pfeil, S.H.; Schuler, B. Microfluidic mixer designed for performing single-molecule kinetics with confocal detection on timescales from milliseconds to minutes. Nat. Protoc. 2013, 8, 1459-1474.
    • (2013) Nat. Protoc. , vol.8 , pp. 1459-1474
    • Wunderlich, B.1    Nettels, D.2    Benke, S.3    Clark, J.4    Weidner, S.5    Hofmann, H.6    Pfeil, S.H.7    Schuler, B.8
  • 71
    • 1542501215 scopus 로고    scopus 로고
    • Dynamics and folding of single two-stranded coiled-coil peptides studied by fluorescent energy transfer confocal microscopy
    • Talaga, D.S.; Lau, W.L.; Roder, H.; Tang, J.Y.; Jia, Y.W.; DeGrado, W.F.; Hochstrasser, R.M. Dynamics and folding of single two-stranded coiled-coil peptides studied by fluorescent energy transfer confocal microscopy. Proc. Natl. Acad. Sci. USA 2000, 97, 13021-13026.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 13021-13026
    • Talaga, D.S.1    Lau, W.L.2    Roder, H.3    Tang, J.Y.4    Jia, Y.W.5    DeGrado, W.F.6    Hochstrasser, R.M.7
  • 72
    • 3042732323 scopus 로고    scopus 로고
    • Multiple states of the tyr318leu mutant of dihydroorotate dehydrogenase revealed by single-molecule kinetics
    • Shi, J.; Palfey, B.A.; Dertouzos, J.; Jensen, K.F.; Gafni, A.; Steel, D. Multiple states of the Tyr318Leu mutant of dihydroorotate dehydrogenase revealed by single-molecule kinetics. J. Am. Chem. Soc. 2004, 126, 6914-6922.
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 6914-6922
    • Shi, J.1    Palfey, B.A.2    Dertouzos, J.3    Jensen, K.F.4    Gafni, A.5    Steel, D.6
  • 74
    • 80055033153 scopus 로고    scopus 로고
    • Single-molecule fluorescence spectroscopy maps the folding landscape of a large protein
    • Pirchi, M.; Ziv, G.; Riven, I.; Cohen, S.S.; Zohar, N.; Barak, Y.; Haran, G. Single-molecule fluorescence spectroscopy maps the folding landscape of a large protein. Nat. Commun. 2011, 2, 493.
    • (2011) Nat. Commun. , vol.2 , pp. 493
    • Pirchi, M.1    Ziv, G.2    Riven, I.3    Cohen, S.S.4    Zohar, N.5    Barak, Y.6    Haran, G.7
  • 75
    • 0031565728 scopus 로고    scopus 로고
    • The foldon universe: A survey of structural similarity and self-recognition of independently folding units
    • Panchenko, A.R.; Luthey Schulten, Z.; Cole, R.; Wolynes, P.G. The foldon universe: A survey of structural similarity and self-recognition of independently folding units. J. Mol. Biol. 1997, 272, 95-105.
    • (1997) J. Mol. Biol. , vol.272 , pp. 95-105
    • Panchenko, A.R.1    Luthey Schulten, Z.2    Cole, R.3    Wolynes, P.G.4
  • 76
    • 84857510185 scopus 로고    scopus 로고
    • Single-molecule fluorescence experiments determine protein folding transition path times
    • Chung, H.S.; McHale, K.; Louis, J.M.; Eaton, W.A. Single-molecule fluorescence experiments determine protein folding transition path times. Science 2012, 335, 981-984.
    • (2012) Science , vol.335 , pp. 981-984
    • Chung, H.S.1    McHale, K.2    Louis, J.M.3    Eaton, W.A.4
  • 78
    • 48249097986 scopus 로고    scopus 로고
    • Intrinsically disordered proteins in human diseases: Introducing the D2 concept
    • Uversky, V.N.; Oldfield, C.J.; Dunker, A.K. Intrinsically disordered proteins in human diseases: Introducing the D2 concept. Annu. Rev. Biophys. 2008, 37, 215-246.
    • (2008) Annu. Rev. Biophys. , vol.37 , pp. 215-246
    • Uversky, V.N.1    Oldfield, C.J.2    Dunker, A.K.3
  • 80
    • 33847324863 scopus 로고    scopus 로고
    • A natively unfolded yeast prion monomer adopts an ensemble of collapsed and rapidly fluctuating structures
    • Mukhopadhyay, S.; Krishnan, R.; Lemke, E.A.; Lindquist, S.; Deniz, A.A. A natively unfolded yeast prion monomer adopts an ensemble of collapsed and rapidly fluctuating structures. Proc. Natl. Acad. Sci. USA 2007, 104, 2649-2654.
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 2649-2654
    • Mukhopadhyay, S.1    Krishnan, R.2    Lemke, E.A.3    Lindquist, S.4    Deniz, A.A.5
  • 81
    • 65249185574 scopus 로고    scopus 로고
    • Interplay of alpha-synuclein binding and conformational switching probed by single-molecule fluorescence
    • Ferreon, A.C.; Gambin, Y.; Lemke, E.A.; Deniz, A.A. Interplay of alpha-synuclein binding and conformational switching probed by single-molecule fluorescence. Proc. Natl. Acad. Sci. USA 2009, 106, 5645-5650.
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 5645-5650
    • Ferreon, A.C.1    Gambin, Y.2    Lemke, E.A.3    Deniz, A.A.4
  • 82
    • 77952328486 scopus 로고    scopus 로고
    • Alteration of the alpha-synuclein folding landscape by a mutation related to parkinson's disease
    • Ferreon, A.C.; Moran, C.R.; Ferreon, J.C.; Deniz, A.A. Alteration of the alpha-synuclein folding landscape by a mutation related to Parkinson's disease. Angew. Chem. Int. Ed. 2010, 49, 3469-3472.
    • (2010) Angew. Chem. Int. Ed. , vol.49 , pp. 3469-3472
    • Ferreon, A.C.1    Moran, C.R.2    Ferreon, J.C.3    Deniz, A.A.4
  • 83
    • 79955685287 scopus 로고    scopus 로고
    • Allostery in a disordered protein: Oxidative modifications to alpha-synuclein act distally to regulate membrane binding
    • Sevcsik, E.; Trexler, A.J.; Dunn, J.M.; Rhoades, E. Allostery in a disordered protein: Oxidative modifications to alpha-synuclein act distally to regulate membrane binding. J. Am. Chem. Soc. 2011, 133, 7152-7158.
    • (2011) J. Am. Chem. Soc. , vol.133 , pp. 7152-7158
    • Sevcsik, E.1    Trexler, A.J.2    Dunn, J.M.3    Rhoades, E.4
  • 84
    • 78249280020 scopus 로고    scopus 로고
    • Single molecule characterization of alpha-synuclein in aggregation-prone states
    • Trexler, A.J.; Rhoades, E. Single molecule characterization of alpha-synuclein in aggregation-prone states. Biophys. J. 2010, 99, 3048-3055.
    • (2010) Biophys. J. , vol.99 , pp. 3048-3055
    • Trexler, A.J.1    Rhoades, E.2
  • 85
    • 80855144832 scopus 로고    scopus 로고
    • A membrane-bound antiparallel dimer of rat islet amyloid polypeptide
    • Nath, A.; Miranker, A.D.; Rhoades, E. A membrane-bound antiparallel dimer of rat islet amyloid polypeptide. Angew. Chem. Int. Ed. 2011, 50, 10859-10862.
    • (2011) Angew. Chem. Int. Ed. , vol.50 , pp. 10859-10862
    • Nath, A.1    Miranker, A.D.2    Rhoades, E.3
  • 86
    • 84867390250 scopus 로고    scopus 로고
    • Identification of an aggregation-prone structure of tau
    • Elbaum-Garfinkle, S.; Rhoades, E. Identification of an aggregation-prone structure of tau. J. Am. Chem. Soc. 2012, 134, 16607-16613.
    • (2012) J. Am. Chem. Soc. , vol.134 , pp. 16607-16613
    • Elbaum-Garfinkle, S.1    Rhoades, E.2
  • 87
    • 84879327823 scopus 로고    scopus 로고
    • Modulation of allostery by protein intrinsic disorder
    • Ferreon, A.C.M.; Ferreon, J.C.; Wright, P.E.; Deniz, A.A. Modulation of allostery by protein intrinsic disorder. Nature 2013, 498, 390-394.
    • (2013) Nature , vol.498 , pp. 390-394
    • Ferreon, A.C.M.1    Ferreon, J.C.2    Wright, P.E.3    Deniz, A.A.4
  • 88
    • 84885455051 scopus 로고    scopus 로고
    • Single-molecule spectroscopy of the unexpected collapse of an unfolded protein at low pH
    • Hofmann, H.; Nettels, D.; Schuler, B. Single-molecule spectroscopy of the unexpected collapse of an unfolded protein at low pH. J. Chem. Phys. 2013, 139, 121930.
    • (2013) J. Chem. Phys. , vol.139
    • Hofmann, H.1    Nettels, D.2    Schuler, B.3
  • 90
    • 84897057069 scopus 로고    scopus 로고
    • Single-molecule studies of intrinsically disordered proteins
    • Brucale, M.; Schuler, B.; Samori, B. Single-molecule studies of intrinsically disordered proteins. Chem. Rev. 2014, 114, 3281-3317.
    • (2014) Chem. Rev. , vol.114 , pp. 3281-3317
    • Brucale, M.1    Schuler, B.2    Samori, B.3
  • 91
    • 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
  • 92
    • 70350340728 scopus 로고    scopus 로고
    • The role of dynamic conformational ensembles in biomolecular recognition
    • Boehr, D.D.; Nussinov, R.; Wright, P.E. The role of dynamic conformational ensembles in biomolecular recognition. Nat. Chem. Biol. 2009, 5, 789-796.
    • (2009) Nat. Chem. Biol. , vol.5 , pp. 789-796
    • Boehr, D.D.1    Nussinov, R.2    Wright, P.E.3
  • 93
  • 94
    • 84857542642 scopus 로고    scopus 로고
    • Taking ockham's razor to enzyme dynamics and catalysis
    • Glowacki, D.R.; Harvey, J.N.; Mulholland, A.J. Taking Ockham's razor to enzyme dynamics and catalysis. Nat. Chem. 2012, 4, 169-176.
    • (2012) Nat. Chem. , vol.4 , pp. 169-176
    • Glowacki, D.R.1    Harvey, J.N.2    Mulholland, A.J.3
  • 95
    • 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
  • 96
    • 47649125643 scopus 로고    scopus 로고
    • Allosteric regulation and catalysis emerge via a common route
    • Goodey, N.M.; Benkovic, S.J. Allosteric regulation and catalysis emerge via a common route. Nat. Chem. Biol. 2008, 4, 474-482.
    • (2008) Nat. Chem. Biol. , vol.4 , pp. 474-482
    • Goodey, N.M.1    Benkovic, S.J.2
  • 97
    • 70450191983 scopus 로고    scopus 로고
    • Dynamic activation of an allosteric regulatory protein
    • Tzeng, S.R.; Kalodimos, C.G. Dynamic activation of an allosteric regulatory protein. Nature 2009, 462, 368-372.
    • (2009) Nature , vol.462 , pp. 368-372
    • Tzeng, S.R.1    Kalodimos, C.G.2
  • 98
    • 77951226274 scopus 로고    scopus 로고
    • At the dawn of the 21st century: Is dynamics the missing link for understanding enzyme catalysis?
    • Kamerlin, S.C.L.; Warshel, A. At the dawn of the 21st century: Is dynamics the missing link for understanding enzyme catalysis? Proteins-Struct. Funct. Bioinf. 2010, 78, 1339-1375.
    • (2010) Proteins-Struct. Funct. Bioinf. , vol.78 , pp. 1339-1375
    • Kamerlin, S.C.L.1    Warshel, A.2
  • 100
    • 61949212626 scopus 로고    scopus 로고
    • The large conformational changes of hsp90 are only weakly coupled to ATP hydrolysis
    • Mickler, M.; Hessling, M.; Ratzke, C.; Buchner, J.; Hugel, T. The large conformational changes of Hsp90 are only weakly coupled to ATP hydrolysis. Nat. Struct. Mol. Bio. 2009, 16, 281-286.
    • (2009) Nat. Struct. Mol. Bio. , vol.16 , pp. 281-286
    • Mickler, M.1    Hessling, M.2    Ratzke, C.3    Buchner, J.4    Hugel, T.5
  • 101
    • 70350453758 scopus 로고    scopus 로고
    • Enzyme millisecond conformational dynamics do not catalyze the chemical step
    • Pisliakov, A.V.; Cao, J.; Kamerlin, S.C.; Warshel, A. Enzyme millisecond conformational dynamics do not catalyze the chemical step. Proc. Natl. Acad. Sci. USA 2009, 106, 17359-17364.
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 17359-17364
    • Pisliakov, A.V.1    Cao, J.2    Kamerlin, S.C.3    Warshel, A.4
  • 102
    • 84879069952 scopus 로고    scopus 로고
    • A single-molecule dissection of ligand binding to a protein with intrinsic dynamics
    • Kim, E.; Lee, S.; Jeon, A.; Choi, J.M.; Lee, H.S.; Hohng, S.; Kim, H.S. A single-molecule dissection of ligand binding to a protein with intrinsic dynamics. Nat. Chem. Biol. 2013, 9, 313-318.
    • (2013) Nat. Chem. Biol. , vol.9 , pp. 313-318
    • Kim, E.1    Lee, S.2    Jeon, A.3    Choi, J.M.4    Lee, H.S.5    Hohng, S.6    Kim, H.S.7
  • 103
    • 84899472221 scopus 로고    scopus 로고
    • Protein conformational dynamics dictate the binding affinity for a ligand
    • Seo, M.H.; Park, J.; Kim, E.; Hohng, S.; Kim, H.S. Protein conformational dynamics dictate the binding affinity for a ligand. Nat. Commun. 2014, 5, doi:10.1038/ncomms4724.
    • (2014) Nat. Commun. , vol.5
    • Seo, M.H.1    Park, J.2    Kim, E.3    Hohng, S.4    Kim, H.S.5
  • 104
    • 78651119908 scopus 로고
    • Measurement of activity of single molecules of beta-D-galactosidase
    • Rotman, B. Measurement of activity of single molecules of beta-D-galactosidase. Proc. Natl. Acad. Sci. USA 1961, 47, 1981-1991.
    • (1961) Proc. Natl. Acad. Sci. USA , vol.47 , pp. 1981-1991
    • Rotman, B.1
  • 105
    • 84855828496 scopus 로고    scopus 로고
    • Cytoplasmic dynein moves through uncoordinated stepping of the AAA+ ring domains
    • DeWitt, M.A.; Chang, A.Y.; Combs, P.A.; Yildiz, A. Cytoplasmic dynein moves through uncoordinated stepping of the AAA+ ring domains. Science 2012, 335, 221-225.
    • (2012) Science , vol.335 , pp. 221-225
    • DeWitt, M.A.1    Chang, A.Y.2    Combs, P.A.3    Yildiz, A.4
  • 108
    • 29844457049 scopus 로고    scopus 로고
    • Conformational dynamics of the isoalloxazine in substrate-free p-hydroxybenzoate hydroxylase: Single-molecule studies
    • Brender, J.R.; Dertouzos, J.; Ballou, D.P.; Massey, V.; Palfey, B.A.; Entsch, B.; Steel, D.G.; Gafni, A. Conformational dynamics of the isoalloxazine in substrate-free p-hydroxybenzoate hydroxylase: Single-molecule studies. J. Am. Chem. Soc. 2005, 127, 18171-18178.
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 18171-18178
    • Brender, J.R.1    Dertouzos, J.2    Ballou, D.P.3    Massey, V.4    Palfey, B.A.5    Entsch, B.6    Steel, D.G.7    Gafni, A.8
  • 109
    • 33645831562 scopus 로고    scopus 로고
    • Single-molecule kinetics reveals signatures of half-sites reactivity in dihydroorotate dehydrogenase A catalysis
    • Shi, J.; Dertouzos, J.; Gafni, A.; Steel, D.; Palfey, B.A. Single-molecule kinetics reveals signatures of half-sites reactivity in dihydroorotate dehydrogenase A catalysis. Proc. Natl. Acad. Sci. USA 2006, 103, 5775-5780.
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 5775-5780
    • Shi, J.1    Dertouzos, J.2    Gafni, A.3    Steel, D.4    Palfey, B.A.5
  • 115
  • 116
    • 0033523011 scopus 로고    scopus 로고
    • Single-molecule enzymology
    • Xie, X.S.; Lu, H.P. Single-molecule Enzymology. J. Biol. Chem. 1999, 274, 15967-15970.
    • (1999) J. Biol. Chem. , vol.274 , pp. 15967-15970
    • Xie, X.S.1    Lu, H.P.2
  • 119
    • 84855284619 scopus 로고    scopus 로고
    • Mixing subattolitre volumes in a quantitative and highly parallel manner with soft matter nanofluidics
    • Christensen, S.M.; Bolinger, P.Y.; Hatzakis, N.S.; Mortensen, M.W.; Stamou, D. Mixing subattolitre volumes in a quantitative and highly parallel manner with soft matter nanofluidics. Nat. Nanotech. 2012, 7, 51-55.
    • (2012) Nat. Nanotech. , vol.7 , pp. 51-55
    • Christensen, S.M.1    Bolinger, P.Y.2    Hatzakis, N.S.3    Mortensen, M.W.4    Stamou, D.5
  • 120
    • 79960286601 scopus 로고    scopus 로고
    • Observation of inhomogeneity in the lipid composition of individual nanoscale liposomes
    • Larsen, J.; Hatzakis, N.S.; Stamou, D. Observation of inhomogeneity in the lipid composition of individual nanoscale liposomes. J. Am. Chem. Soc. 2011, 133, 10685-10687.
    • (2011) J. Am. Chem. Soc. , vol.133 , pp. 10685-10687
    • Larsen, J.1    Hatzakis, N.S.2    Stamou, D.3
  • 122
    • 77950596030 scopus 로고    scopus 로고
    • A unifying mechanism accounts for sensing of membrane curvature by BAR domains, amphipathic helices and membrane-anchored proteins
    • Bhatia, V.K.; Hatzakis, N.S.; Stamou, D. A unifying mechanism accounts for sensing of membrane curvature by BAR domains, amphipathic helices and membrane-anchored proteins. Semin. Cell Dev. Biol. 2010, 21, 381-390.
    • (2010) Semin. Cell Dev. Biol. , vol.21 , pp. 381-390
    • Bhatia, V.K.1    Hatzakis, N.S.2    Stamou, D.3
  • 123
    • 71549146572 scopus 로고    scopus 로고
    • Constructing size distributions of liposomes from single-object fluorescence measurements
    • Lohr, C.; Kunding, A.H.; Bhatia, V.K.; Stamou, D. Constructing size distributions of liposomes from single-object fluorescence measurements. Methods Enzymol. 2009, 465, 143-160.
    • (2009) Methods Enzymol. , vol.465 , pp. 143-160
    • Lohr, C.1    Kunding, A.H.2    Bhatia, V.K.3    Stamou, D.4
  • 125
    • 68149120533 scopus 로고    scopus 로고
    • Quantification of nano-scale intermembrane contact areas by using fluorescence resonance energy transfer
    • Bendix, P.M.; Pedersen, M.S.; Stamou, D. Quantification of nano-scale intermembrane contact areas by using fluorescence resonance energy transfer. Proc. Natl. Acad. Sci. USA 2009, 106, 12341-12346.
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 12341-12346
    • Bendix, P.M.1    Pedersen, M.S.2    Stamou, D.3
  • 126
    • 78149432825 scopus 로고    scopus 로고
    • Laboratory evolution of stereoselective enzymes: A prolific source of catalysts for asymmetric reactions
    • Reetz, M.T. Laboratory evolution of stereoselective enzymes: A prolific source of catalysts for asymmetric reactions. Angew. Chem. Int. Ed. 2011, 50, 138-174.
    • (2011) Angew. Chem. Int. Ed. , vol.50 , pp. 138-174
    • Reetz, M.T.1
  • 127
    • 0037450115 scopus 로고    scopus 로고
    • Ferulic acid esterase from humicola insolens catalyzes enantioselective transesterification of secondary alcohols
    • Hatzakis, N.S.; Daphnomili, D.; Smonou, I. Ferulic acid esterase from Humicola Insolens catalyzes enantioselective transesterification of secondary alcohols. J. Mol. Catal. B: Enzym. 2003, 21, 309-311.
    • (2003) J. Mol. Catal. B: Enzym. , vol.21 , pp. 309-311
    • Hatzakis, N.S.1    Daphnomili, D.2    Smonou, I.3
  • 128
    • 21844442117 scopus 로고    scopus 로고
    • Asymmetric transesterification of secondary alcohols catalyzed by feruloyl esterase from humicola insolens
    • Hatzakis, N.S.; Smonou, I. Asymmetric transesterification of secondary alcohols catalyzed by feruloyl esterase from Humicola insolens. Bioorg. Chem. 2005, 33, 325-337.
    • (2005) Bioorg. Chem. , vol.33 , pp. 325-337
    • Hatzakis, N.S.1    Smonou, I.2
  • 129
    • 0032479388 scopus 로고    scopus 로고
    • Lipases: Interfacial enzymes with attractive applications
    • Schmid, R.D.; Verger, R. Lipases: Interfacial enzymes with attractive applications. Angew. Chem. Int. Ed. 1998, 37, 1609-1633.
    • (1998) Angew. Chem. Int. Ed. , vol.37 , pp. 1609-1633
    • Schmid, R.D.1    Verger, R.2
  • 130
    • 1542298842 scopus 로고    scopus 로고
    • Enantioselectivity and diastereoselectivity in the transesterification of secondary alcohols mediated by feruloyl esterase from humicola insolens
    • Hatzakis, N.S.; Smonou, I. Enantioselectivity and diastereoselectivity in the transesterification of secondary alcohols mediated by feruloyl esterase from Humicola insolens. Tetrahedron Lett. 2004, 45, 2755-2757.
    • (2004) Tetrahedron Lett. , vol.45 , pp. 2755-2757
    • Hatzakis, N.S.1    Smonou, I.2
  • 132
    • 68049111471 scopus 로고    scopus 로고
    • Finding better protein engineering strategies
    • Kazlauskas, R.J.; Bornscheuer, U.T. Finding better protein engineering strategies. Nat. Chem. Biol. 2009, 5, 526-529.
    • (2009) Nat. Chem. Biol. , vol.5 , pp. 526-529
    • Kazlauskas, R.J.1    Bornscheuer, U.T.2
  • 133
    • 3142769080 scopus 로고    scopus 로고
    • Origins of delays in monolayer kinetics: Phospholipase A(2) paradigm
    • Cajal, Y.; Berg, O.G.; Jain, M.K. Origins of delays in monolayer kinetics: Phospholipase A(2) paradigm. Biochemistry 2004, 43, 9256-9264.
    • (2004) Biochemistry , vol.43 , pp. 9256-9264
    • Cajal, Y.1    Berg, O.G.2    Jain, M.K.3
  • 134
    • 77951903021 scopus 로고    scopus 로고
    • Membrane protein assembly into nanodiscs
    • Bayburt, T.H.; Sligar, S.G. Membrane protein assembly into nanodiscs. FEBS Lett. 2010, 584, 1721-1727.
    • (2010) FEBS Lett. , vol.584 , pp. 1721-1727
    • Bayburt, T.H.1    Sligar, S.G.2
  • 135
    • 78649450474 scopus 로고    scopus 로고
    • Conformational changes of the NADPH-dependent cytochrome P450 reductase in the course of electron transfer to cytochromes P450
    • Laursen, T.; Jensen, K.; Møller, B.L. Conformational changes of the NADPH-dependent cytochrome P450 reductase in the course of electron transfer to cytochromes P450. Biochim. Biophys. Acta 2011, 1814, 132-138.
    • (2011) Biochim. Biophys. Acta , vol.1814 , pp. 132-138
    • Laursen, T.1    Jensen, K.2    Møller, B.L.3
  • 136
    • 73649131594 scopus 로고    scopus 로고
    • Plant NADPH-cytochrome P450 oxidoreductases
    • Jensen, K.; Møller, B.L. Plant NADPH-cytochrome P450 oxidoreductases. Phytochemistry 2010, 71, 132-141.
    • (2010) Phytochemistry , vol.71 , pp. 132-141
    • Jensen, K.1    Møller, B.L.2
  • 138
    • 40349092943 scopus 로고    scopus 로고
    • Genetics of P450 oxidoreductase: Sequence variation in 842 individuals of four ethnicities and activities of 15 missense mutations
    • Huang, N.; Agrawal, V.; Giacomini, K.M.; Miller, W.L. Genetics of P450 oxidoreductase: Sequence variation in 842 individuals of four ethnicities and activities of 15 missense mutations. Proc. Natl. Acad. Sci. USA 2008, 105, 1733-1738.
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 1733-1738
    • Huang, N.1    Agrawal, V.2    Giacomini, K.M.3    Miller, W.L.4
  • 140
    • 38649113858 scopus 로고    scopus 로고
    • Multiscale complex network of protein conformational fluctuations in single-molecule time series
    • Li, C.B.; Yang, H.; Kornatsuzaki, T. Multiscale complex network of protein conformational fluctuations in single-molecule time series. Proc. Natl. Acad. Sci. USA 2008, 105, 536-541.
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 536-541
    • Li, C.B.1    Yang, H.2    Kornatsuzaki, T.3
  • 141
    • 64849113665 scopus 로고    scopus 로고
    • Trapping moving targets with small molecules
    • Lee, G.M.; Craik, C.S. Trapping moving targets with small molecules. Science 2009, 324, 213-215.
    • (2009) Science , vol.324 , pp. 213-215
    • Lee, G.M.1    Craik, C.S.2
  • 142
    • 33748619206 scopus 로고    scopus 로고
    • An NMR perspective on enzyme dynamics
    • Boehr, D.D.; Dyson, H.J.; Wright, P.E. An NMR perspective on enzyme dynamics. Chem. Rev. 2006, 106, 3055-3079.
    • (2006) Chem. Rev. , vol.106 , pp. 3055-3079
    • Boehr, D.D.1    Dyson, H.J.2    Wright, P.E.3
  • 143
    • 64849111005 scopus 로고    scopus 로고
    • Sending signals dynamically
    • Smock, R.G.; Gierasch, L.M. Sending Signals Dynamically. Science 2009, 324, 198-203.
    • (2009) Science , vol.324 , pp. 198-203
    • Smock, R.G.1    Gierasch, L.M.2
  • 145
    • 1542327706 scopus 로고    scopus 로고
    • Single-molecule and transient kinetics investigation of the interaction of dihydrofolate reductase with NADPH and dihydrofolate
    • Zhang, Z.Q.; Rajagopalan, P.T.R.; Selzer, T.; Benkovic, S.J.; Hammes, G.G. Single-molecule and transient kinetics investigation of the interaction of dihydrofolate reductase with NADPH and dihydrofolate. Proc. Natl. Acad. Sci. USA 2004, 101, 2764-2769.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 2764-2769
    • Zhang, Z.Q.1    Rajagopalan, P.T.R.2    Selzer, T.3    Benkovic, S.J.4    Hammes, G.G.5
  • 146
    • 23344450919 scopus 로고    scopus 로고
    • Functional conformational motions in the turnover cycle of cholesterol oxidase
    • Lerch, H.P.; Rigler, R.; Mikhailov, A.S. Functional conformational motions in the turnover cycle of cholesterol oxidase. Proc. Natl. Acad. Sci. USA 2005, 102, 10807-10812.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 10807-10812
    • Lerch, H.P.1    Rigler, R.2    Mikhailov, A.S.3
  • 149
    • 0037180453 scopus 로고    scopus 로고
    • Conformational-relaxation models of single-enzyme kinetics
    • Lerch, H.P.; Mikhailov, A.S.; Hess, B. Conformational-relaxation models of single-enzyme kinetics. Proc. Natl. Acad. Sci. USA 2002, 99, 15410-15415.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 15410-15415
    • Lerch, H.P.1    Mikhailov, A.S.2    Hess, B.3
  • 151
    • 84873450232 scopus 로고    scopus 로고
    • Time-resolved single molecule fluorescence spectroscopy of an alpha-chymotrypsin catalyzed reaction
    • Terentyeva, T.G.; Hofkens, J.; Komatsuzaki, T.; Blank, K.; Li, C.B. Time-resolved single molecule fluorescence spectroscopy of an alpha-Chymotrypsin catalyzed reaction. J. Phys. Chem. B 2013, 117, 1252-1260.
    • (2013) J. Phys. Chem. B , vol.117 , pp. 1252-1260
    • Terentyeva, T.G.1    Hofkens, J.2    Komatsuzaki, T.3    Blank, K.4    Li, C.B.5
  • 153
    • 58149265181 scopus 로고    scopus 로고
    • Toolbox for analyzing finite two-state trajectories
    • Flomenbom, O.; Silbey, R.J. Toolbox for analyzing finite two-state trajectories. Phys. Rev. E 2008, 78, doi:10.1103/PhysRevE.78.066105.
    • (2008) Phys. Rev. E , vol.78
    • Flomenbom, O.1    Silbey, R.J.2
  • 154
    • 77957754309 scopus 로고    scopus 로고
    • Enzyme dynamics point to stepwise conformational selection in catalysis
    • Ma, B.Y.; Nussinov, R. Enzyme dynamics point to stepwise conformational selection in catalysis. Curr. Opin. Chem. Biol. 2010, 14, 652-659.
    • (2010) Curr. Opin. Chem. Biol. , vol.14 , pp. 652-659
    • Ma, B.Y.1    Nussinov, R.2
  • 155
    • 68049085675 scopus 로고    scopus 로고
    • A 21(st) century revisionist's view at a turning point in enzymology
    • Nagel, Z.D.; Klinman, J.P. A 21(st) 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
  • 157
    • 0035937443 scopus 로고    scopus 로고
    • Two-state allosteric behavior in a single-domain signaling protein
    • Volkman, B.F.; Lipson, D.; Wemmer, D.E.; Kern, D. Two-state allosteric behavior in a single-domain signaling protein. Science 2001, 291, 2429-2433.
    • (2001) Science , vol.291 , pp. 2429-2433
    • Volkman, B.F.1    Lipson, D.2    Wemmer, D.E.3    Kern, D.4
  • 158
    • 0028934277 scopus 로고
    • Differences in the chemical reactivity of individual molecules of an enzyme
    • Xue, Q.F.; Yeung, E.S. Differences in the chemical reactivity of individual molecules of an enzyme. Nature 1995, 373, 681-683.
    • (1995) Nature , vol.373 , pp. 681-683
    • Xue, Q.F.1    Yeung, E.S.2
  • 159
    • 0034709430 scopus 로고    scopus 로고
    • Single molecules of highly purified bacterial alkaline phosphatase have identical activity
    • Polakowski, R.; Craig, D.B.; Skelley, A.; Dovichi, N.J. Single molecules of highly purified bacterial alkaline phosphatase have identical activity. J. Am. Chem. Soc. 2000, 122, 4853-4855.
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 4853-4855
    • Polakowski, R.1    Craig, D.B.2    Skelley, A.3    Dovichi, N.J.4
  • 160
    • 35448981947 scopus 로고    scopus 로고
    • Stochastic inhibitor release and binding from single-enzyme molecules
    • Gorris, H.H.; Rissin, D.M.; Walt, D.R. Stochastic inhibitor release and binding from single-enzyme molecules. Proc. Natl. Acad. Sci. USA 2007, 104, 17680-17685.
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 17680-17685
    • Gorris, H.H.1    Rissin, D.M.2    Walt, D.R.3
  • 161
    • 84907020126 scopus 로고    scopus 로고
    • Observing single enzyme molecules interconvert between activity states upon heating
    • Rojek, M.J.; Walt, D.R. Observing single enzyme molecules interconvert between activity states upon heating. PLoS One 2014, 9, doi:10.1371/journal.pone.0086224.
    • (2014) PLoS One , vol.9
    • Rojek, M.J.1    Walt, D.R.2
  • 162
    • 76249126156 scopus 로고    scopus 로고
    • Multiple native states reveal persistent ruggedness of an RNA folding landscape
    • Solomatin, S.V.; Greenfeld, M.; Chu, S.; Herschlag, D. Multiple native states reveal persistent ruggedness of an RNA folding landscape. Nature 2010, 463, 681-687.
    • (2010) Nature , vol.463 , pp. 681-687
    • Solomatin, S.V.1    Greenfeld, M.2    Chu, S.3    Herschlag, D.4
  • 163
    • 70450242805 scopus 로고    scopus 로고
    • Exploring protein fitness landscapes by directed evolution
    • Romero, P.A.; Arnold, F.H. Exploring protein fitness landscapes by directed evolution. Nat. Rev. Mol. Cell Biol. 2009, 10, 866-876.
    • (2009) Nat. Rev. Mol. Cell Biol. , vol.10 , pp. 866-876
    • Romero, P.A.1    Arnold, F.H.2
  • 164
    • 84899494694 scopus 로고    scopus 로고
    • A single molecule perspective on the functional diversity of in vitro evolved beta-glucuronidase
    • Liebherr, R.B.; Renner, M.; Gorris, H.H. A Single molecule perspective on the functional diversity of In vitro evolved beta-Glucuronidase. J. Am. Chem. Soc. 2014, 136, 5949-5955.
    • (2014) J. Am. Chem. Soc. , vol.136 , pp. 5949-5955
    • Liebherr, R.B.1    Renner, M.2    Gorris, H.H.3
  • 165
    • 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
  • 170
    • 55449101108 scopus 로고    scopus 로고
    • Beta-cyclodextrin-appended giant amphiphile: Aggregation to vesicle polymersomes and immobilisation of enzymes
    • Felici, M.; Marza-Perez, M.; Hatzakis, N.S.; Nolte, R.J.M.; Feiters, M.C. beta-Cyclodextrin-appended giant amphiphile: Aggregation to vesicle polymersomes and immobilisation of enzymes. Chem. Eur. J. 2008, 14, 9914-9920.
    • (2008) Chem. Eur. J. , vol.14 , pp. 9914-9920
    • Felici, M.1    Marza-Perez, M.2    Hatzakis, N.S.3    Nolte, R.J.M.4    Feiters, M.C.5
  • 173
  • 176
    • 79959936612 scopus 로고    scopus 로고
    • Single-molecule approach to immunoprecipitated protein complexes: Insights into miRNA uridylation
    • Yeom, K.H.; Heo, I.; Lee, J.; Hohng, S.; Kim, V.N.; Joo, C. Single-molecule approach to immunoprecipitated protein complexes: Insights into miRNA uridylation. EMBO Rep. 2011, 12, 690-696.
    • (2011) EMBO Rep. , vol.12 , pp. 690-696
    • Yeom, K.H.1    Heo, I.2    Lee, J.3    Hohng, S.4    Kim, V.N.5    Joo, C.6
  • 177
    • 84867081368 scopus 로고    scopus 로고
    • A general approach to break the concentration barrier in single-molecule imaging
    • Loveland, A.B.; Habuchi, S.; Walter, J.C.; van Oijen, A.M. A general approach to break the concentration barrier in single-molecule imaging. Nat. Methods 2012, 9, 987-992.
    • (2012) Nat. Methods , vol.9 , pp. 987-992
    • Loveland, A.B.1    Habuchi, S.2    Walter, J.C.3    Van Oijen, A.M.4
  • 178
    • 0000096835 scopus 로고    scopus 로고
    • Click chemistry: Diverse chemical function from a few good reactions
    • Kolb, H.C.; Finn, M.G.; Sharpless, K.B. Click chemistry: Diverse chemical function from a few good reactions. Angew. Chem. Int. Ed. 2001, 40, 2004-2021.
    • (2001) Angew. Chem. Int. Ed. , vol.40 , pp. 2004-2021
    • Kolb, H.C.1    Finn, M.G.2    Sharpless, K.B.3
  • 179
    • 84898072114 scopus 로고    scopus 로고
    • Bioorthogonal reactions for labeling proteins
    • Lang, K.; Chin, J.W. Bioorthogonal reactions for labeling proteins. ACS Chem. Biol. 2014, 9, 16-20.
    • (2014) ACS Chem. Biol. , vol.9 , pp. 16-20
    • Lang, K.1    Chin, J.W.2
  • 182
    • 0037012920 scopus 로고    scopus 로고
    • Peptidotriazoles on solid phase: [1,2,3]-triazoles by regiospecific copper(i)-catalyzed 1,3-dipolar cycloadditions of terminal alkynes to azides
    • Tornøe, C.W.; Christensen, C.; Meldal, M. Peptidotriazoles on solid phase: [1,2,3]-Triazoles by regiospecific copper(i)-catalyzed 1,3-dipolar cycloadditions of terminal alkynes to azides. J. Org. Chem. 2002, 67, 3057-3064.
    • (2002) J. Org. Chem. , vol.67 , pp. 3057-3064
    • Tornøe, C.W.1    Christensen, C.2    Meldal, M.3
  • 184
    • 84857445877 scopus 로고    scopus 로고
    • Genetically encoded norbornene directs site-specific cellular protein labelling via a rapid bioorthogonal reaction
    • Lang, K.; Davis, L.; Torres-Kolbus, J.; Chou, C.; Deiters, A.; Chin, J.W. Genetically encoded norbornene directs site-specific cellular protein labelling via a rapid bioorthogonal reaction. Nat. Chem. 2012, 4, 298-304.
    • (2012) Nat. Chem. , vol.4 , pp. 298-304
    • Lang, K.1    Davis, L.2    Torres-Kolbus, J.3    Chou, C.4    Deiters, A.5    Chin, J.W.6
  • 186
    • 84886636226 scopus 로고    scopus 로고
    • Comparative analysis of click chemistry mediated activity-based protein profiling in cell lysates
    • Yang, Y.; Yang, X.; Verhelst, S. Comparative analysis of click chemistry mediated activity-based protein profiling in cell lysates. Molecules 2013, 18, 12599-12608.
    • (2013) Molecules , vol.18 , pp. 12599-12608
    • Yang, Y.1    Yang, X.2    Verhelst, S.3
  • 187
    • 33750295496 scopus 로고    scopus 로고
    • Nonblinking and long-lasting single-molecule fluorescence imaging
    • Rasnik, I.; McKinney, S.A.; Ha, T. Nonblinking and long-lasting single-molecule fluorescence imaging. Nat. Methods 2006, 3, 891-893.
    • (2006) Nat. Methods , vol.3 , pp. 891-893
    • Rasnik, I.1    McKinney, S.A.2    Ha, T.3
  • 188
    • 84878890467 scopus 로고    scopus 로고
    • Small-molecule photostabilizing agents are modifiers of lipid bilayer properties
    • Alejo, J.L.; Blanchard, S.C.; Andersen, O.S. Small-molecule photostabilizing agents are modifiers of lipid bilayer properties. Biophys. J. 2013, 104, 2410-2418.
    • (2013) Biophys. J. , vol.104 , pp. 2410-2418
    • Alejo, J.L.1    Blanchard, S.C.2    Andersen, O.S.3
  • 190
    • 84860352408 scopus 로고    scopus 로고
    • "Self-healing" dyes: Intramolecular stabilization of organic fluorophores
    • author reply 427-428
    • Tinnefeld, P.; Cordes, T. "Self-healing" dyes: Intramolecular stabilization of organic fluorophores. Nat. Methods 2012, 9, 426-427; author reply 427-428.
    • (2012) Nat. Methods , vol.9 , pp. 426-427
    • Tinnefeld, P.1    Cordes, T.2
  • 194
    • 2942650138 scopus 로고    scopus 로고
    • Fluorescence-aided molecule sorting: Analysis of structure and interactions by alternating-laser excitation of single molecules
    • Kapanidis, A.N.; Lee, N.K.; Laurence, T.A.; Doose, S.; Margeat, E.; Weiss, S. Fluorescence-aided molecule sorting: Analysis of structure and interactions by alternating-laser excitation of single molecules. Proc. Natl. Acad. Sci. USA 2004, 101, 8936-8941.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 8936-8941
    • Kapanidis, A.N.1    Lee, N.K.2    Laurence, T.A.3    Doose, S.4    Margeat, E.5    Weiss, S.6
  • 196
    • 4143071283 scopus 로고    scopus 로고
    • Single-molecule three-color FRET
    • Hohng, S.; Joo, C.; Ha, T. Single-molecule three-color FRET. Biophys. J. 2004, 87, 1328-1337.
    • (2004) Biophys. J. , vol.87 , pp. 1328-1337
    • Hohng, S.1    Joo, C.2    Ha, T.3
  • 200
    • 84878684586 scopus 로고    scopus 로고
    • Direct imaging of single UvrD helicase dynamics on long single-stranded DNA
    • Lee, K.S.; Balci, H.; Jia, H.; Lohman, T.M.; Ha, T. Direct imaging of single UvrD helicase dynamics on long single-stranded DNA. Nat. Commun. 2013, 4, 1878.
    • (2013) Nat. Commun. , vol.4 , pp. 1878
    • Lee, K.S.1    Balci, H.2    Jia, H.3    Lohman, T.M.4    Ha, T.5
  • 201
    • 33645033645 scopus 로고    scopus 로고
    • Probing gene expression in live cells, one protein molecule at a time
    • Yu, J.; Xiao, J.; Ren, X.J.; Lao, K.Q.; Xie, X.S. Probing gene expression in live cells, one protein molecule at a time. Science 2006, 311, 1600-1603.
    • (2006) Science , vol.311 , pp. 1600-1603
    • Yu, J.1    Xiao, J.2    Ren, X.J.3    Lao, K.Q.4    Xie, X.S.5
  • 204
    • 0037666888 scopus 로고    scopus 로고
    • Implications of protein flexibility for drug discovery
    • Teague, S.J. Implications of protein flexibility for drug discovery. Nat. Rev. Drug Discov. 2003, 2, 527-541.
    • (2003) Nat. Rev. Drug Discov. , vol.2 , pp. 527-541
    • Teague, S.J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.