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Volumn 96, Issue 8, 2009, Pages 1053-1070

Early events in protein folding

Author keywords

Cooperativity; Intermediate; Polypeptide chain collapse; Protein folding; Specificity

Indexed keywords


EID: 70349139155     PISSN: 00113891     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Review
Times cited : (23)

References (221)
  • 2
    • 0002006297 scopus 로고
    • Are there pathways for protein folding?
    • Levinthal, C., Are there pathways for protein folding? J. Chem. Phys., 1968, 65, 44-45.
    • (1968) J. Chem. Phys. , vol.65 , pp. 44-45
    • Levinthal, C.1
  • 4
    • 33744937937 scopus 로고    scopus 로고
    • Early events in protein folding explored by rapid mixing methods
    • Roder, H., Maki, K. and Cheng, H., Early events in protein folding explored by rapid mixing methods. Chem. Rev., 2006, 106, 1836-1861.
    • (2006) Chem. Rev. , vol.106 , pp. 1836-1861
    • Roder, H.1    Maki, K.2    Cheng, H.3
  • 5
    • 33846917230 scopus 로고    scopus 로고
    • Ultrafast and downhill protein folding
    • Dyer, R. B., Ultrafast and downhill protein folding. Curr. Opin. Struct. Biol., 2007, 17, 38-47.
    • (2007) Curr. Opin. Struct. Biol. , vol.17 , pp. 38-47
    • Dyer, R.B.1
  • 7
    • 0015920746 scopus 로고
    • Stages in the mechanism of self-organization of protein molecules
    • Ptitsyn, O. B., Stages in the mechanism of self-organization of protein molecules. Dokl. Akad. Nauk. SSSR, 1973, 210, 1213-1215.
    • (1973) Dokl. Akad. Nauk. SSSR , vol.210 , pp. 1213-1215
    • Ptitsyn, O.B.1
  • 8
    • 0020024242 scopus 로고
    • Specific intermediates in the folding reactions of small proteins and the mechanism of protein folding
    • Kim, P. S. and 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
  • 9
    • 0023758305 scopus 로고
    • NMR evidence for an early framework intermediate on the folding pathway of ribonuclease A
    • Udgaonkar, J. B. and Baldwin, R. L., NMR evidence for an early framework intermediate on the folding pathway of ribonuclease A. Nature, 1988, 335, 694-699.
    • (1988) Nature , vol.335 , pp. 694-699
    • Udgaonkar, J.B.1    Baldwin, R.L.2
  • 10
    • 0017251893 scopus 로고
    • Protein-folding dynamics
    • Karplus, M. and Weaver, D. L., Protein-folding dynamics. Nature, 1976, 260, 404-406.
    • (1976) Nature , vol.260 , pp. 404-406
    • Karplus, M.1    Weaver, D.L.2
  • 11
    • 0024264819 scopus 로고
    • Diffusion-collision model for the folding kinetics of myoglobin
    • Bashford, D., Cohen, F. E., Karplus, M., Kuntz, I. D. and Weaver, D. L., Diffusion-collision model for the folding kinetics of myoglobin. Proteins, 1988, 4, 211-227.
    • (1988) Proteins , vol.4 , pp. 211-227
    • Bashford, D.1    Cohen, F.E.2    Karplus, M.3    Kuntz, I.D.4    Weaver, D.L.5
  • 12
    • 0028327236 scopus 로고
    • Protein folding dynamics: the diffusion-collision model and experimental data
    • Karplus, M. and Weaver, D. L., Protein folding dynamics: the diffusion-collision model and experimental data. Protein Sci., 1994, 3, 650-668.
    • (1994) Protein Sci. , vol.3 , pp. 650-668
    • Karplus, M.1    Weaver, D.L.2
  • 13
    • 0015243226 scopus 로고
    • Analysis of the code relating sequence to conformation in proteins: possible implications for the mechanism of formation of helical regions
    • Robson, B. and Pain, R. H., Analysis of the code relating sequence to conformation in proteins: possible implications for the mechanism of formation of helical regions. J. Mol. Biol., 1971, 58, 237-259.
    • (1971) J. Mol. Biol. , vol.58 , pp. 237-259
    • Robson, B.1    Pain, R.H.2
  • 14
    • 0022423920 scopus 로고
    • Theory for the folding and stability of globular proteins
    • Dill, K. A., Theory for the folding and stability of globular proteins. Biochemistry, 1985, 24, 1501-1509.
    • (1985) Biochemistry , vol.24 , pp. 1501-1509
    • Dill, K.A.1
  • 15
    • 0028944346 scopus 로고
    • Is burst hydrophobic collapse necessary for protein folding?
    • Gutin, A. M., Abkevich, V. I. and Shakhnovich, E. I., Is burst hydrophobic collapse necessary for protein folding? Biochemistry, 1995, 34, 3066-3076.
    • (1995) Biochemistry , vol.34 , pp. 3066-3076
    • Gutin, A.M.1    Abkevich, V.I.2    Shakhnovich, E.I.3
  • 16
    • 0015597839 scopus 로고
    • Nucleation, rapid folding and globular intrachain regions in proteins
    • Wetlaufer, D. B., Nucleation, rapid folding and globular intrachain regions in proteins. Proc. Natl. Acad. Sci. USA, 1973, 70, 697-701.
    • (1973) Proc. Natl. Acad. Sci. USA , vol.70 , pp. 697-701
    • Wetlaufer, D.B.1
  • 17
    • 0028856785 scopus 로고
    • Optimization of rates of protein folding: the nucleation-condensation mechanism and its implications
    • Fersht, A. R., Optimization of rates of protein folding: the nucleation-condensation mechanism and its implications. Proc. Natl. Acad. Sci. USA, 1995, 92, 10869-10873.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 10869-10873
    • Fersht, A.R.1
  • 18
    • 0037221599 scopus 로고    scopus 로고
    • Is there a unifying mechanism for protein folding?
    • Daggett, V. and Fersht, A. R., Is there a unifying mechanism for protein folding? Trends Biochem. Sci., 2003, 28, 18-25.
    • (2003) Trends Biochem. Sci. , vol.28 , pp. 18-25
    • Daggett, V.1    Fersht, A.R.2
  • 19
    • 0031815749 scopus 로고    scopus 로고
    • How do small single-domain proteins fold?
    • Jackson, S. E., How do small single-domain proteins fold? Fold Des., 1998, 3, R81-R91.
    • (1998) Fold Des. , vol.3
    • Jackson, S.E.1
  • 20
    • 0028947257 scopus 로고
    • Funnels, pathways, and the energy landscape of protein folding: a synthesis
    • Bryngelson, J. D., Onuchic, J. N., Socci, N. D. and 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
  • 21
    • 1842298212 scopus 로고    scopus 로고
    • From Levinthal to pathways to funnels
    • Dill, K. A. and Chan, H. S., From Levinthal to pathways to funnels. Nature Struct. Biol., 1997, 4, 10-19.
    • (1997) Nature Struct. Biol. , vol.4 , pp. 10-19
    • Dill, K.A.1    Chan, H.S.2
  • 22
    • 0029053552 scopus 로고
    • Folding of a nascent polypeptide chain in vitro: cooperative formation of structure in a protein module
    • De Prat Gay, G., Ruiz-Sanz, J., Neira, J. L., Itzhaki, L. S. and Fersht, A. R., Folding of a nascent polypeptide chain in vitro: cooperative formation of structure in a protein module. Proc. Natl. Acad. Sci. USA, 1995, 92, 3683-3686.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 3683-3686
    • De Prat Gay, G.1    Ruiz-Sanz, J.2    Neira, J.L.3    Itzhaki, L.S.4    Fersht, A.R.5
  • 23
    • 0028802181 scopus 로고
    • Initial hydrophobic collapse in the folding of barstar
    • Agashe, V. R., Shastry, M. C. and Udgaonkar, J. B., Initial hydrophobic collapse in the folding of barstar. Nature, 1995, 377, 754-757.
    • (1995) Nature , vol.377 , pp. 754-757
    • Agashe, V.R.1    Shastry, M.C.2    Udgaonkar, J.B.3
  • 27
    • 11144236111 scopus 로고    scopus 로고
    • Ultrarapid mixing experiments shed new light on the characteristics of the initial conformational ensemble during the folding of ribonuclease A
    • Welker, E., Maki, K., Shastry, M. C., Juminaga, D., Bhat, R., Scheraga, H. A. and Roder, H., Ultrarapid mixing experiments shed new light on the characteristics of the initial conformational ensemble during the folding of ribonuclease A. Proc. Natl. Acad. Sci. USA, 2004, 101, 17681-17686.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 17681-17686
    • Welker, E.1    Maki, K.2    Shastry, M.C.3    Juminaga, D.4    Bhat, R.5    Scheraga, H.A.6    Roder, H.7
  • 28
    • 33947315248 scopus 로고    scopus 로고
    • Microsecond hydrophobic collapse in the folding of Escherichia coli dihydrofolate reductase, an alpha/beta-type protein
    • Arai, M., Kondrashkina, E., Kayatekin, C., Matthews, C. R., Iwakura, M. and Bilsel, O., Microsecond hydrophobic collapse in the folding of Escherichia coli dihydrofolate reductase, an alpha/beta-type protein. J. Mol. Biol., 2007, 368, 219-229.
    • (2007) J. Mol. Biol. , vol.368 , pp. 219-229
    • Arai, M.1    Kondrashkina, E.2    Kayatekin, C.3    Matthews, C.R.4    Iwakura, M.5    Bilsel, O.6
  • 29
    • 0032978994 scopus 로고    scopus 로고
    • Chain collapse can occur concomitantly with the rate-limiting step in protein folding
    • Plaxco, K. W., Millett, I. S., Segel, D. J., Doniach, S. and Baker, D., Chain collapse can occur concomitantly with the rate-limiting step in protein folding. Nature Struct. Biol., 1999, 6, 554-556.
    • (1999) Nature Struct. Biol. , vol.6 , pp. 554-556
    • Plaxco, K.W.1    Millett, I.S.2    Segel, D.J.3    Doniach, S.4    Baker, D.5
  • 30
    • 0036535895 scopus 로고    scopus 로고
    • Protein folding: the free energy surface
    • Gruebele, M., Protein folding: the free energy surface. Curr. Opin. Struct. Biol., 2002, 12, 161-168.
    • (2002) Curr. Opin. Struct. Biol. , vol.12 , pp. 161-168
    • Gruebele, M.1
  • 32
    • 0028901085 scopus 로고
    • The folding mechanism of barstar: evidence for multiple pathways and multiple intermediates
    • Shastry, M. C. and Udgaonkar, J. B., The folding mechanism of barstar: evidence for multiple pathways and multiple intermediates. J. Mol. Biol., 1995, 247, 1013-1027.
    • (1995) J. Mol. Biol. , vol.247 , pp. 1013-1027
    • Shastry, M.C.1    Udgaonkar, J.B.2
  • 33
    • 0030473296 scopus 로고    scopus 로고
    • Kinetic intermediates in the formation of the cytochrome c molten globule
    • Colon, W. and Roder, H., Kinetic intermediates in the formation of the cytochrome c molten globule. Nature Struct. Biol., 1996, 3, 1019-1025.
    • (1996) Nature Struct. Biol. , vol.3 , pp. 1019-1025
    • Colon, W.1    Roder, H.2
  • 34
    • 35448932093 scopus 로고    scopus 로고
    • Characterization of the folding and unfolding reactions of single-chain monellin: evidence for multiple intermediates and competing pathways
    • Patra, A. K. and Udgaonkar, J. B., Characterization of the folding and unfolding reactions of single-chain monellin: evidence for multiple intermediates and competing pathways. Biochemistry, 2007, 46, 11727-11743.
    • (2007) Biochemistry , vol.46 , pp. 11727-11743
    • Patra, A.K.1    Udgaonkar, J.B.2
  • 35
    • 0033551522 scopus 로고    scopus 로고
    • Observation of multistate kinetics during the slow folding and unfolding of barstar
    • Bhuyan, A. K. and Udgaonkar, J. B., Observation of multistate kinetics during the slow folding and unfolding of barstar. Biochemistry, 1999, 38, 9158-9168.
    • (1999) Biochemistry , vol.38 , pp. 9158-9168
    • Bhuyan, A.K.1    Udgaonkar, J.B.2
  • 38
    • 26244466045 scopus 로고    scopus 로고
    • Dependence of the size of the initially collapsed form during the refolding of barstar on denaturant concentration: evidence for a continuous transition
    • Sinha, K. K. and Udgaonkar, J. B., Dependence of the size of the initially collapsed form during the refolding of barstar on denaturant concentration: evidence for a continuous transition. J. Mol. Biol., 2005, 353, 704-718.
    • (2005) J. Mol. Biol. , vol.353 , pp. 704-718
    • Sinha, K.K.1    Udgaonkar, J.B.2
  • 39
    • 33746102627 scopus 로고    scopus 로고
    • Atom-by-atom analysis of global downhill protein folding
    • Sadqi, M., Fushman, D. and Munoz, V., Atom-by-atom analysis of global downhill protein folding. Nature, 2006, 442, 317-321.
    • (2006) Nature , vol.442 , pp. 317-321
    • Sadqi, M.1    Fushman, D.2    Munoz, V.3
  • 40
    • 34249748424 scopus 로고    scopus 로고
    • Dissecting the non-specific and specific components of the initial folding reaction of barstar by multi-site FRET measurements
    • Sinha, K. K. and Udgaonkar, J. B., Dissecting the non-specific and specific components of the initial folding reaction of barstar by multi-site FRET measurements. J. Mol. Biol., 2007, 370, 385-405.
    • (2007) J. Mol. Biol. , vol.370 , pp. 385-405
    • Sinha, K.K.1    Udgaonkar, J.B.2
  • 41
    • 0001804089 scopus 로고    scopus 로고
    • Aspects of protein reaction dynamics: deviations from simple behaviour
    • B104
    • Karplus, M., Aspects of protein reaction dynamics: deviations from simple behaviour. J. Phys. Chem., 2000, B104, 11-27.
    • (2000) J. Phys. Chem. , pp. 11-27
    • Karplus, M.1
  • 42
    • 0033060613 scopus 로고    scopus 로고
    • Searching for 'downhill scenarios' in protein folding
    • Eaton, W. A., Searching for 'downhill scenarios' in protein folding. Proc. Natl. Acad. Sci. USA, 1999, 96, 5897-5899.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 5897-5899
    • Eaton, W.A.1
  • 43
    • 34347218159 scopus 로고    scopus 로고
    • Conformational dynamics and ensembles in protein folding
    • Munoz, V., Conformational dynamics and ensembles in protein folding. Annu. Rev. Biophys. Biomol. Struct., 2007, 36, 395-412.
    • (2007) Annu. Rev. Biophys. Biomol. Struct. , vol.36 , pp. 395-412
    • Munoz, V.1
  • 44
    • 0038329308 scopus 로고    scopus 로고
    • Folding at the speed limit
    • Yang, W. Y. and Gruebele, M., Folding at the speed limit. Nature, 2003, 423, 193-197.
    • (2003) Nature , vol.423 , pp. 193-197
    • Yang, W.Y.1    Gruebele, M.2
  • 46
    • 34948869804 scopus 로고    scopus 로고
    • The ultimate speed limit to protein folding is conformational searching
    • Ghosh, K., Ozkan, S. B. and Dill, K. A., The ultimate speed limit to protein folding is conformational searching. J. Am. Chem. Soc., 2007, 129, 11920-11927.
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 11920-11927
    • Ghosh, K.1    Ozkan, S.B.2    Dill, K.A.3
  • 47
    • 1842454986 scopus 로고    scopus 로고
    • Fast and faster: a designed variant of the B-domain of protein A folds in 3 microsec
    • Arora, P., Oas, T. G. and Myers, J. K., Fast and faster: a designed variant of the B-domain of protein A folds in 3 microsec. Protein Sci., 2004, 13, 847-853.
    • (2004) Protein Sci. , vol.13 , pp. 847-853
    • Arora, P.1    Oas, T.G.2    Myers, J.K.3
  • 48
    • 25144462746 scopus 로고    scopus 로고
    • Ultra-fast barrier-limited folding in the peripheral subunit-binding domain family
    • Ferguson, N. et al., Ultra-fast barrier-limited folding in the peripheral subunit-binding domain family. J. Mol. Biol., 2005, 353, 427-446.
    • (2005) J. Mol. Biol. , vol.353 , pp. 427-446
    • Ferguson, N.1
  • 49
    • 34547151184 scopus 로고    scopus 로고
    • The helix-turn-helix motif as an ultrafast independently folding domain: the pathway of folding of Engrailed homeodomain
    • Religa, T. L., Johnson, C. M., Vu, D. M., Brewer, S. H., Dyer, R. B. and Fersht, A. R., The helix-turn-helix motif as an ultrafast independently folding domain: the pathway of folding of Engrailed homeodomain. Proc. Natl. Acad. Sci. USA, 2007, 104, 9272-9277.
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 9272-9277
    • Religa, T.L.1    Johnson, C.M.2    Vu, D.M.3    Brewer, S.H.4    Dyer, R.B.5    Fersht, A.R.6
  • 52
    • 23944522022 scopus 로고    scopus 로고
    • Downhill protein folding: evolution meets physics
    • Gruebele, M., Downhill protein folding: evolution meets physics. C. R. Biol., 2005, 328, 701-712.
    • (2005) C. R. Biol , vol.328 , pp. 701-712
    • Gruebele, M.1
  • 53
    • 14044258768 scopus 로고    scopus 로고
    • Kinetics are probe-dependent during downhill folding of an engineered lambda6-85 protein
    • Ma, H. and Gruebele, M., Kinetics are probe-dependent during downhill folding of an engineered lambda6-85 protein. Proc. Natl. Acad. Sci. USA, 2005, 102, 2283-2287.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 2283-2287
    • Ma, H.1    Gruebele, M.2
  • 54
    • 38549129313 scopus 로고    scopus 로고
    • Comments on probe-dependent and independent relaxation kinetics: unreliable signatures of downhill folding
    • Gruebele, M., Comments on probe-dependent and independent relaxation kinetics: unreliable signatures of downhill folding. Proteins, 2007, 70, 1099-1102.
    • (2007) Proteins , vol.70 , pp. 1099-1102
    • Gruebele, M.1
  • 55
    • 34249887411 scopus 로고    scopus 로고
    • Probe-dependent and nonexponential relaxation kinetics: unreliable signatures of downhill protein folding
    • Hagen, S. J., Probe-dependent and nonexponential relaxation kinetics: unreliable signatures of downhill protein folding. Proteins, 2007, 68, 205-217.
    • (2007) Proteins , vol.68 , pp. 205-217
    • Hagen, S.J.1
  • 56
    • 3042814557 scopus 로고    scopus 로고
    • Folding lambda-repressor at its speed limit
    • Yang, W. Y. and Gruebele, M., Folding lambda-repressor at its speed limit. Biophys. J., 2004, 87, 596-608.
    • (2004) Biophys. J. , vol.87 , pp. 596-608
    • Yang, W.Y.1    Gruebele, M.2
  • 57
    • 38349117215 scopus 로고    scopus 로고
    • Origins of barriers and barrierless folding in BBL
    • Cho, S. S., Weinkam, P. and Wolynes, P. G., Origins of barriers and barrierless folding in BBL. Proc. Natl. Acad. Sci. USA, 2008, 105, 118-123.
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 118-123
    • Cho, S.S.1    Weinkam, P.2    Wolynes, P.G.3
  • 58
    • 33846073474 scopus 로고    scopus 로고
    • Distinguishing between cooperative and unimodal downhill protein folding
    • Huang, F., Sato, S., Sharpe, T. D., Ying, L. and Fersht, A. R., Distinguishing between cooperative and unimodal downhill protein folding. Proc. Natl. Acad. Sci. USA, 2007, 104, 123-127.
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 123-127
    • Huang, F.1    Sato, S.2    Sharpe, T.D.3    Ying, L.4    Fersht, A.R.5
  • 59
    • 36749012371 scopus 로고    scopus 로고
    • Relaxation rate for an ultrfast folding protein is independent of chemical denaturant concentration
    • Cellmer, T., Henry, E. R., Kubelka, J., Hofrichter, J. and Eaton, W. A., Relaxation rate for an ultrfast folding protein is independent of chemical denaturant concentration. J. Am. Chem. Soc., 2007, 129, 14564-14565.
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 14564-14565
    • Cellmer, T.1    Henry, E.R.2    Kubelka, J.3    Hofrichter, J.4    Eaton, W.A.5
  • 60
  • 61
    • 33847795209 scopus 로고    scopus 로고
    • Loop formation in unfolded polypeptide chains on the picoseconds to microseconds time scale
    • Fierz, B., Satzger, H., Root, C., Gilch, P., Zinth, W. and Kiefhaber, T., Loop formation in unfolded polypeptide chains on the picoseconds to microseconds time scale. Proc. Natl. Acad. Sci. USA, 2007, 104, 2163-2168.
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 2163-2168
    • Fierz, B.1    Satzger, H.2    Root, C.3    Gilch, P.4    Zinth, W.5    Kiefhaber, T.6
  • 62
    • 0034691198 scopus 로고    scopus 로고
    • Measuring the rate of intramolecular contact formation in polypeptides
    • Lapidus, L. J., Eaton, W. A. and Hofrichter, J., Measuring the rate of intramolecular contact formation in polypeptides. Proc. Natl. Acad. Sci. USA, 2000, 97, 7220-7225.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 7220-7225
    • Lapidus, L.J.1    Eaton, W.A.2    Hofrichter, J.3
  • 63
    • 0035793222 scopus 로고    scopus 로고
    • Rate of intrachain contact formation in an unfolded protein: temperature and denaturant effects
    • Hagen, S. J., Carswell, C. W. and Sjolander, E. M., Rate of intrachain contact formation in an unfolded protein: temperature and denaturant effects. J. Mol. Biol., 2001, 305, 1161-1171.
    • (2001) J. Mol. Biol. , vol.305 , pp. 1161-1171
    • Hagen, S.J.1    Carswell, C.W.2    Sjolander, E.M.3
  • 64
    • 55649096822 scopus 로고    scopus 로고
    • The intrinsic stiffness of polyglutamine peptides
    • Singh, V. R. and Lapidus, L. J., The intrinsic stiffness of polyglutamine peptides. J. Phys. Chem. B, 2008, 112, 13172-13176.
    • (2008) J. Phys. Chem. B , vol.112 , pp. 13172-13176
    • Singh, V.R.1    Lapidus, L.J.2
  • 65
    • 0038502170 scopus 로고    scopus 로고
    • Folding dynamics and mechanism of beta-hairpin formation
    • Munoz, V., Thompson, P. A., Hofrichter, J. and Eaton, W. A., Folding dynamics and mechanism of beta-hairpin formation. Nature, 1997, 390, 196-199.
    • (1997) Nature , vol.390 , pp. 196-199
    • Munoz, V.1    Thompson, P.A.2    Hofrichter, J.3    Eaton, W.A.4
  • 66
    • 0033536452 scopus 로고    scopus 로고
    • Alpha-helix peptide folding and unfolding activation barriers: a nanosecond UV resonance Raman study
    • Lednev, I. K., Karnoup, A. S., Sparrow, M. C. and Asher, S. A., Alpha-helix peptide folding and unfolding activation barriers: a nanosecond UV resonance Raman study. J. Am. Chem. Soc., 1999, 121, 8074-8086.
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 8074-8086
    • Lednev, I.K.1    Karnoup, A.S.2    Sparrow, M.C.3    Asher, S.A.4
  • 69
    • 0037143694 scopus 로고    scopus 로고
    • The ensemble folding kinetics of protein G from an all-atom Monte Carlo simulation
    • Shimada, J. and Shakhnovich, E. I., The ensemble folding kinetics of protein G from an all-atom Monte Carlo simulation. Proc. Natl. Acad. Sci. USA, 2002, 99, 11175-11180.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 11175-11180
    • Shimada, J.1    Shakhnovich, E.I.2
  • 70
    • 4644261149 scopus 로고    scopus 로고
    • Osmolytes induce structure in an early intermediate on the folding pathway of barstar
    • Pradeep, L. and Udgaonkar, J. B., Osmolytes induce structure in an early intermediate on the folding pathway of barstar. J. Biol. Chem., 2004, 279, 40303-40313.
    • (2004) J. Biol. Chem. , vol.279 , pp. 40303-40313
    • Pradeep, L.1    Udgaonkar, J.B.2
  • 71
    • 1542358783 scopus 로고    scopus 로고
    • Increasing stability reduces conformational heterogeneity in a protein folding intermediate ensemble
    • Sridevi, K., Lakshmikanth, G. S., Krishnamoorthy, G. and Udgaonkar, J. B., Increasing stability reduces conformational heterogeneity in a protein folding intermediate ensemble. J. Mol. Biol., 2004, 337, 699-711.
    • (2004) J. Mol. Biol. , vol.337 , pp. 699-711
    • Sridevi, K.1    Lakshmikanth, G.S.2    Krishnamoorthy, G.3    Udgaonkar, J.B.4
  • 72
    • 10044269982 scopus 로고    scopus 로고
    • Many faces of the unfolded state: conformational heterogeneity in denatured yeast cytochrome C
    • Pletneva, E. V., Gray, H. B. and Winkler, J. R., Many faces of the unfolded state: conformational heterogeneity in denatured yeast cytochrome C. J. Mol. Biol., 2005, 345, 855-867.
    • (2005) J. Mol. Biol. , vol.345 , pp. 855-867
    • Pletneva, E.V.1    Gray, H.B.2    Winkler, J.R.3
  • 73
    • 0027190920 scopus 로고
    • Structure and stability of an early folding intermediate of Escherichia coli trp aporepressor measured by far-UV stopped-flow circular dichroism and 8-anilino-1-naphthalene sulfonate binding
    • Mann, C. J. and Matthews, C. R., Structure and stability of an early folding intermediate of Escherichia coli trp aporepressor measured by far-UV stopped-flow circular dichroism and 8-anilino-1-naphthalene sulfonate binding. Biochemistry, 1993, 32, 5282-5290.
    • (1993) Biochemistry , vol.32 , pp. 5282-5290
    • Mann, C.J.1    Matthews, C.R.2
  • 75
    • 0032512697 scopus 로고    scopus 로고
    • Kinetics of lysozyme refolding: structural characterization of a non-specifically collapsed state using timeresolved X-ray scattering
    • Chen, L., Wildegger, G., Kiefhaber, T., Hodgson, K. O. and Doniach, S., Kinetics of lysozyme refolding: structural characterization of a non-specifically collapsed state using timeresolved X-ray scattering. J. Mol. Biol., 1998, 276, 225-237.
    • (1998) J. Mol. Biol. , vol.276 , pp. 225-237
    • Chen, L.1    Wildegger, G.2    Kiefhaber, T.3    Hodgson, K.O.4    Doniach, S.5
  • 76
    • 0036440985 scopus 로고    scopus 로고
    • Fast and slow intermediate accumulation and the initial barrier mechanism in protein folding
    • Krantz, B. A., Mayne, L., Rumbley, J., Englander, S. W. and Sosnick, T. R., Fast and slow intermediate accumulation and the initial barrier mechanism in protein folding. J. Mol. Biol., 2002, 324, 359-371.
    • (2002) J. Mol. Biol. , vol.324 , pp. 359-371
    • Krantz, B.A.1    Mayne, L.2    Rumbley, J.3    Englander, S.W.4    Sosnick, T.R.5
  • 78
    • 0030599429 scopus 로고    scopus 로고
    • Temperature-jump induced fast refolding of cold-unfolded protein
    • Nolting, B., Temperature-jump induced fast refolding of cold-unfolded protein. Biochem. Biophys. Res. Commun., 1996, 227, 903-908.
    • (1996) Biochem. Biophys. Res. Commun. , vol.227 , pp. 903-908
    • Nolting, B.1
  • 79
    • 70349113632 scopus 로고    scopus 로고
    • Wiley-VCH: Weiheim, 1st edn
    • Gruebele, M., Fast Relaxation Methods, Wiley-VCH: Weiheim, 2005, 1st edn, vol. 1, p. 572.
    • (2005) Fast Relaxation Methods , vol.1 , pp. 572
    • Gruebele, M.1
  • 80
    • 0030596513 scopus 로고    scopus 로고
    • 13C NMR assignment and characterisation of residual structure
    • 13C NMR assignment and characterisation of residual structure. J. Mol. Biol., 1996, 259, 805-818.
    • (1996) J. Mol. Biol. , vol.259 , pp. 805-818
    • Wong, K.B.1    Freund, S.M.2    Fersht, A.R.3
  • 81
    • 0343580520 scopus 로고    scopus 로고
    • Circular dichroism of denatured barstar suggests residual structure
    • Nolting, B., Golbik, R., Soler-Gonzalez, A. S. and Fersht, A. R., Circular dichroism of denatured barstar suggests residual structure. Biochemistry, 1997, 36, 9899-9905.
    • (1997) Biochemistry , vol.36 , pp. 9899-9905
    • Nolting, B.1    Golbik, R.2    Soler-Gonzalez, A.S.3    Fersht, A.R.4
  • 82
    • 0027131947 scopus 로고
    • Fast events in protein folding initiated by nanosecond laser photolysis
    • Jones, C. M. et al., Fast events in protein folding initiated by nanosecond laser photolysis. Proc. Natl. Acad. Sci. USA, 1993, 90, 11860-11864.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 11860-11864
    • Jones, C.M.1
  • 83
    • 0029964867 scopus 로고    scopus 로고
    • Diffusion-limited contact formation in unfolded cytochrome c: estimating the maximum rate of protein folding
    • Hagen, S. J., Hofrichter, J., Szabo, A. and Eaton, W. A., Diffusion-limited contact formation in unfolded cytochrome c: estimating the maximum rate of protein folding. Proc. Natl. Acad. Sci. USA, 1996, 93, 11615-11617.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 11615-11617
    • Hagen, S.J.1    Hofrichter, J.2    Szabo, A.3    Eaton, W.A.4
  • 84
    • 22244435625 scopus 로고    scopus 로고
    • Protein dynamics control proton transfer from bulk solvent to protein interior: a case study with a green fluorescent protein
    • Saxena, A. M., Udgaonkar, J. B. and Krishnamoorthy, G., Protein dynamics control proton transfer from bulk solvent to protein interior: a case study with a green fluorescent protein. Protein Sci., 2005, 14, 1787-1799.
    • (2005) Protein Sci , vol.14 , pp. 1787-1799
    • Saxena, A.M.1    Udgaonkar, J.B.2    Krishnamoorthy, G.3
  • 87
    • 0031919973 scopus 로고    scopus 로고
    • Evidence for barrier-limited protein folding kinetics on the microsecond time scale
    • Shastry, M. C. and Roder, H., Evidence for barrier-limited protein folding kinetics on the microsecond time scale. Nature Struct. Biol., 1998, 5, 385-392.
    • (1998) Nature Struct. Biol. , vol.5 , pp. 385-392
    • Shastry, M.C.1    Roder, H.2
  • 88
    • 0032867418 scopus 로고    scopus 로고
    • Folding dynamics of the B1 domain of protein G explored by ultrarapid mixing
    • Park, S. H., Shastry, M. C. and Roder, H., Folding dynamics of the B1 domain of protein G explored by ultrarapid mixing. Nature Struct. Biol., 1999, 6, 943-947.
    • (1999) Nature Struct. Biol. , vol.6 , pp. 943-947
    • Park, S.H.1    Shastry, M.C.2    Roder, H.3
  • 89
    • 34447292770 scopus 로고    scopus 로고
    • Protein hydrophobic collapse and early folding steps observed in a microfluidic mixer
    • Lapidus, L. J., Yao, S., McGarrity, K. S., Hertzog, D. E., Tubman, E. and Bakajin, O., Protein hydrophobic collapse and early folding steps observed in a microfluidic mixer. Biophys. J., 2007, 93, 218-224.
    • (2007) Biophys. J. , vol.93 , pp. 218-224
    • Lapidus, L.J.1    Yao, S.2    McGarrity, K.S.3    Hertzog, D.E.4    Tubman, E.5    Bakajin, O.6
  • 90
    • 45849127598 scopus 로고    scopus 로고
    • Barrierless evolution of structure during the sub-ms refolding reaction of a small protein
    • Sinha, K. K. and Udgaonkar, J. B., Barrierless evolution of structure during the sub-ms refolding reaction of a small protein. Proc. Natl. Acad. Sci. USA, 2008, 105, 7998-8003.
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 7998-8003
    • Sinha, K.K.1    Udgaonkar, J.B.2
  • 91
    • 34247144594 scopus 로고    scopus 로고
    • A rapid flow mixer with 11-ms mixing time microfabricated by a pulsed-laser ablation technique: observation of a barrier-limited collapse in cytochrome c folding
    • Matsumoto, S., Yane, A., Nakashima, S., Hashida, M., Fujita, M., Goto, Y. and Takahashi, S., A rapid flow mixer with 11-ms mixing time microfabricated by a pulsed-laser ablation technique: observation of a barrier-limited collapse in cytochrome c folding. J. Am. Chem. Soc., 2007, 129, 3840-3841.
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 3840-3841
    • Matsumoto, S.1    Yane, A.2    Nakashima, S.3    Hashida, M.4    Fujita, M.5    Goto, Y.6    Takahashi, S.7
  • 93
    • 0028935887 scopus 로고
    • Structure and stability of monomeric lambda repressor: NMR evidence for two-state folding
    • Huang, G. S. and Oas, T. G., Structure and stability of monomeric lambda repressor: NMR evidence for two-state folding. Biochemistry, 1995, 34, 3884-3892.
    • (1995) Biochemistry , vol.34 , pp. 3884-3892
    • Huang, G.S.1    Oas, T.G.2
  • 94
    • 4344570150 scopus 로고    scopus 로고
    • NMR studies of protein folding
    • Juneja, J. and Udgaonkar, J. B., NMR studies of protein folding. Curr. Sci., 2003, 84, 157-172.
    • (2003) Curr. Sci. , vol.84 , pp. 157-172
    • Juneja, J.1    Udgaonkar, J.B.2
  • 95
    • 0037126290 scopus 로고    scopus 로고
    • Probing the free-energy surface for protein folding with single-molecule fluorescence spectroscopy
    • Schuler, B., Lipman, E. A. and 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
  • 96
    • 0041321045 scopus 로고    scopus 로고
    • Single-molecule measurement of protein folding kinetics
    • Lipman, E. A., Schuler, B., Bakajin, O. and 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
  • 97
    • 46749116409 scopus 로고    scopus 로고
    • Non-equilibrium single molecule protein folding in a co-axial mixer
    • Hamadani, K. M. and Weiss, S., Non-equilibrium single molecule protein folding in a co-axial mixer. Biophys. J., 2008, 95, 352-365.
    • (2008) Biophys. J. , vol.95 , pp. 352-365
    • Hamadani, K.M.1    Weiss, S.2
  • 98
    • 33746823043 scopus 로고    scopus 로고
    • Coil-globule transition in the denatured state of a small protein
    • Sherman, E. and Haran, G., Coil-globule transition in the denatured state of a small protein. Proc. Natl. Acad. Sci. USA, 2006, 103, 11539-11543.
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 11539-11543
    • Sherman, E.1    Haran, G.2
  • 99
    • 34547529763 scopus 로고    scopus 로고
    • Dynamics of equilibrium structural fluctuations of apomyoglobin measured by fluorescence correlation spectroscopy
    • Chen, H., Rhoades, E., Butler, J. S., Loh, S. N. and Webb, W. W., Dynamics of equilibrium structural fluctuations of apomyoglobin measured by fluorescence correlation spectroscopy. Proc. Natl. Acad. Sci. USA, 2007, 104, 10459-10464.
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 10459-10464
    • Chen, H.1    Rhoades, E.2    Butler, J.S.3    Loh, S.N.4    Webb, W.W.5
  • 100
    • 1542513548 scopus 로고    scopus 로고
    • Force-clamp spectroscopy monitors the folding trajectory of a single protein
    • Fernandez, J. M. and Li, H., Force-clamp spectroscopy monitors the folding trajectory of a single protein. Science, 2004, 303, 1674-1678.
    • (2004) Science , vol.303 , pp. 1674-1678
    • Fernandez, J.M.1    Li, H.2
  • 101
    • 25444512161 scopus 로고    scopus 로고
    • Direct observation of the three-state folding of a single protein molecule
    • Cecconi, C., Shank, E. A., Bustamante, C. and Marqusee, S., Direct observation of the three-state folding of a single protein molecule. Science, 2005, 309, 2057-2060.
    • (2005) Science , vol.309 , pp. 2057-2060
    • Cecconi, C.1    Shank, E.A.2    Bustamante, C.3    Marqusee, S.4
  • 103
    • 33645223271 scopus 로고    scopus 로고
    • Suppressing Brownian motion of individual biomolecules in solution
    • Cohen, A. E. and Moerner, W. E., Suppressing Brownian motion of individual biomolecules in solution. Proc. Natl. Acad. Sci. USA, 2006, 103, 4362-4365.
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 4362-4365
    • Cohen, A.E.1    Moerner, W.E.2
  • 104
    • 34547512144 scopus 로고    scopus 로고
    • Development of a technique for the investigation of folding dynamics of single proteins for extended time periods
    • Kinoshita, M., Kamagata, K., Maeda, A., Goto, Y., Komatsuzaki, T. and Takahashi, S., Development of a technique for the investigation of folding dynamics of single proteins for extended time periods. Proc. Natl. Acad. Sci. USA, 2007, 104, 10453-10458.
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 10453-10458
    • Kinoshita, M.1    Kamagata, K.2    Maeda, A.3    Goto, Y.4    Komatsuzaki, T.5    Takahashi, S.6
  • 105
    • 1842298212 scopus 로고    scopus 로고
    • From Levinthal to pathways to funnels
    • Dill, K. A. and Chan, H. S., From Levinthal to pathways to funnels. Nature Struct. Biol., 1997, 4, 10-19.
    • (1997) Nature Struct. Biol. , vol.4 , pp. 10-19
    • Dill, K.A.1    Chan, H.S.2
  • 107
    • 0025856806 scopus 로고
    • Denatured states of proteins
    • Dill, K. A. and Shortle, D., Denatured states of proteins. Annu. Rev. Biochem., 1991, 60, 795-825.
    • (1991) Annu. Rev. Biochem. , vol.60 , pp. 795-825
    • Dill, K.A.1    Shortle, D.2
  • 109
    • 0035830438 scopus 로고    scopus 로고
    • Distributions of intramolecular distances in the reduced and denatured states of bovine pancreatic ribonuclease A. Folding initiation structures in the C-terminal portions of the reduced protein
    • Navon, A., Ittah, V., Landsman, P., Scheraga, H. A. and Haas, E., Distributions of intramolecular distances in the reduced and denatured states of bovine pancreatic ribonuclease A. Folding initiation structures in the C-terminal portions of the reduced protein. Biochemistry, 2001, 40, 105-118.
    • (2001) Biochemistry , vol.40 , pp. 105-118
    • Navon, A.1    Ittah, V.2    Landsman, P.3    Scheraga, H.A.4    Haas, E.5
  • 110
    • 0014027356 scopus 로고
    • Proteins in 6-M guanidine hydrochloride. Demonstration of random coil behaviour
    • Tanford, C., Kawahara, K. and Lapanje, S., Proteins in 6-M guanidine hydrochloride. Demonstration of random coil behaviour. J. Biol. Chem., 1966, 241, 1921-1923.
    • (1966) J. Biol. Chem. , vol.241 , pp. 1921-1923
    • Tanford, C.1    Kawahara, K.2    Lapanje, S.3
  • 111
    • 4344716256 scopus 로고    scopus 로고
    • Random-coil behaviour and the dimensions of chemically unfolded proteins
    • Kohn, J. E. et al., Random-coil behaviour and the dimensions of chemically unfolded proteins. Proc. Natl. Acad. Sci. USA, 2004, 101, 12491-12496.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 12491-12496
    • Kohn, J.E.1
  • 112
    • 0033730431 scopus 로고    scopus 로고
    • The Flory isolated-pair hypothesis is not valid for polypeptide chains: implications for protein folding
    • Pappu, R. V., Srinivasan, R. and Rose, G. D., The Flory isolated-pair hypothesis is not valid for polypeptide chains: implications for protein folding. Proc. Natl. Acad. Sci. USA, 2000, 97, 12565-12570.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 12565-12570
    • Pappu, R.V.1    Srinivasan, R.2    Rose, G.D.3
  • 113
    • 0033582680 scopus 로고    scopus 로고
    • Probing residual structure and backbone dynamics on the millito picosecond timescale in a urea-denatured fibronectin type III domain
    • Meekhof, A. E. and Freund, S. M., Probing residual structure and backbone dynamics on the millito picosecond timescale in a urea-denatured fibronectin type III domain. J. Mol. Biol., 1999, 286, 579-592.
    • (1999) J. Mol. Biol. , vol.286 , pp. 579-592
    • Meekhof, A.E.1    Freund, S.M.2
  • 114
    • 9344227330 scopus 로고    scopus 로고
    • Native and nonnative conformational preferences in the ureaunfolded state of barstar
    • Bhavesh, N. S., Juneja, J., Udgaonkar, J. B. and Hosur, R. V., Native and nonnative conformational preferences in the ureaunfolded state of barstar. Protein Sci., 2004, 13, 3085-3091.
    • (2004) Protein Sci. , vol.13 , pp. 3085-3091
    • Bhavesh, N.S.1    Juneja, J.2    Udgaonkar, J.B.3    Hosur, R.V.4
  • 115
    • 0026672305 scopus 로고
    • NMR determination of residual structure in a urea-denatured protein, the 434-repressor
    • Neri, D., Billeter, M., Wider, G. and Wuthrich, K., NMR determination of residual structure in a urea-denatured protein, the 434-repressor. Science, 1992, 257, 1559-1563.
    • (1992) Science , vol.257 , pp. 1559-1563
    • Neri, D.1    Billeter, M.2    Wider, G.3    Wuthrich, K.4
  • 116
    • 0028297302 scopus 로고
    • Structural characterization of the FK506 binding protein unfolded in urea and guanidine hydrochloride
    • Logan, T. M., Theriault, Y. and Fesik, S. W., Structural characterization of the FK506 binding protein unfolded in urea and guanidine hydrochloride. J. Mol. Biol., 1994, 236, 637-648.
    • (1994) J. Mol. Biol. , vol.236 , pp. 637-648
    • Logan, T.M.1    Theriault, Y.2    Fesik, S.W.3
  • 117
    • 0035936551 scopus 로고    scopus 로고
    • Intestinal fatty acid binding protein: the folding mechanism as determined by NMR studies
    • Hodsdon, M. E. and Frieden, C., Intestinal fatty acid binding protein: the folding mechanism as determined by NMR studies. Biochemistry, 2001, 40, 732-742.
    • (2001) Biochemistry , vol.40 , pp. 732-742
    • Hodsdon, M.E.1    Frieden, C.2
  • 118
    • 0035919635 scopus 로고    scopus 로고
    • Persistence of native-like topology in a denatured protein in 8 M urea
    • Shortle, D. and Ackerman, M. S., Persistence of native-like topology in a denatured protein in 8 M urea. Science, 2001, 293, 487-489.
    • (2001) Science , vol.293 , pp. 487-489
    • Shortle, D.1    Ackerman, M.S.2
  • 119
    • 0037159208 scopus 로고    scopus 로고
    • Molecular hinges in protein folding: the urea-denatured state of apomyoglobin
    • Schwarzinger, S., Wright, P. E. and Dyson, H. J., Molecular hinges in protein folding: the urea-denatured state of apomyoglobin. Biochemistry, 2002, 41, 12681-12686.
    • (2002) Biochemistry , vol.41 , pp. 12681-12686
    • Schwarzinger, S.1    Wright, P.E.2    Dyson, H.J.3
  • 121
    • 33646171099 scopus 로고    scopus 로고
    • Characterization of intra-molecular distances and site-specific dynamics in chemically unfolded barstar: evidence for denaturant-dependent non-random structure
    • Saxena, A. M., Udgaonkar, J. B. and Krishnamoorthy, G., Characterization of intra-molecular distances and site-specific dynamics in chemically unfolded barstar: evidence for denaturant-dependent non-random structure. J. Mol. Biol., 2006, 359, 174-189.
    • (2006) J. Mol. Biol. , vol.359 , pp. 174-189
    • Saxena, A.M.1    Udgaonkar, J.B.2    Krishnamoorthy, G.3
  • 122
    • 4344704080 scopus 로고    scopus 로고
    • Reassessing random-coil statistics in unfolded proteins
    • Fitzkee, N. C. and Rose, G. D., Reassessing random-coil statistics in unfolded proteins. Proc. Natl. Acad. Sci. USA, 2004, 101, 12497-12502.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 12497-12502
    • Fitzkee, N.C.1    Rose, G.D.2
  • 123
    • 18244364614 scopus 로고    scopus 로고
    • Long-range interactions within a nonnative protein
    • Klein-Seetharaman, J. et al., Long-range interactions within a nonnative protein. Science, 2002, 295, 17119-17122.
    • (2002) Science , vol.295 , pp. 17119-17122
    • Klein-Seetharaman, J.1
  • 124
    • 34247577665 scopus 로고    scopus 로고
    • A pre-existing hydrophobic collapse in the unfolded state of an ultrafast folding protein
    • Mok, K. H., Kuhn, L. T., Goez, M., Day, I. J., Lin, J. C., Andersen, N. H. and Hore, P. J., A pre-existing hydrophobic collapse in the unfolded state of an ultrafast folding protein. Nature, 2007, 447, 106-109.
    • (2007) Nature , vol.447 , pp. 106-109
    • Mok, K.H.1    Kuhn, L.T.2    Goez, M.3    Day, I.J.4    Lin, J.C.5    Andersen, N.H.6    Hore, P.J.7
  • 125
    • 0035957221 scopus 로고    scopus 로고
    • NMR structural and dynamic characterization of the acid-unfolded state of apomyoglobin provides insights into the early events in protein folding
    • Yao, J., Chung, J., Eliezer, D., Wright, P. E. and Dyson, H. J., NMR structural and dynamic characterization of the acid-unfolded state of apomyoglobin provides insights into the early events in protein folding. Biochemistry, 2001, 40, 3561-3571.
    • (2001) Biochemistry , vol.40 , pp. 3561-3571
    • Yao, J.1    Chung, J.2    Eliezer, D.3    Wright, P.E.4    Dyson, H.J.5
  • 126
    • 0034628913 scopus 로고    scopus 로고
    • Towards a complete description of the structural and dynamic properties of the denatured state of barnase and the role of residual structure in folding
    • Wong, K. B., Clarke, J., Bond, C. J., Neira, J. L., Freund, S. M., Fersht, A. R. and Daggett, V., Towards a complete description of the structural and dynamic properties of the denatured state of barnase and the role of residual structure in folding. J. Mol. Biol., 2000, 296, 1257-1282.
    • (2000) J. Mol. Biol. , vol.296 , pp. 1257-1282
    • Wong, K.B.1    Clarke, J.2    Bond, C.J.3    Neira, J.L.4    Freund, S.M.5    Fersht, A.R.6    Daggett, V.7
  • 127
    • 3242789489 scopus 로고    scopus 로고
    • Structural characterization of unfolded states of apomyoglobin using residual dipolar couplings
    • Mohana-Borges, R., Goto, N. K., Kroon, G. J., Dyson, H. J. and Wright, P. E., Structural characterization of unfolded states of apomyoglobin using residual dipolar couplings. J. Mol. Biol., 2004, 340, 1131-1142.
    • (2004) J. Mol. Biol. , vol.340 , pp. 1131-1142
    • Mohana-Borges, R.1    Goto, N.K.2    Kroon, G.J.3    Dyson, H.J.4    Wright, P.E.5
  • 128
    • 0030330918 scopus 로고    scopus 로고
    • Insights into protein folding from NMR
    • Dyson, H. J. and Wright, P. E., Insights into protein folding from NMR. Annu. Rev. Phys. Chem., 1996, 47, 369-395.
    • (1996) Annu. Rev. Phys. Chem. , vol.47 , pp. 369-395
    • Dyson, H.J.1    Wright, P.E.2
  • 129
    • 0035836687 scopus 로고    scopus 로고
    • Protein folding from a highly disordered denatured state: the folding pathway of chymotrypsin inhibitor 2 at atomic resolution
    • Kazmirski, S. L., Wong, K. B., Freund, S. M., Tan, Y. J., Fersht, A. R. and Daggett, V., Protein folding from a highly disordered denatured state: the folding pathway of chymotrypsin inhibitor 2 at atomic resolution. Proc. Natl. Acad. Sci. USA, 2001, 98, 4349-4354.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 4349-4354
    • Kazmirski, S.L.1    Wong, K.B.2    Freund, S.M.3    Tan, Y.J.4    Fersht, A.R.5    Daggett, V.6
  • 130
    • 27344452885 scopus 로고    scopus 로고
    • Single-molecule Forster resonance energy transfer study of protein dynamics under denaturing conditions
    • Kuzmenkina, E. V., Heyes, C. D. and Nienhaus, G. U., Single-molecule Forster resonance energy transfer study of protein dynamics under denaturing conditions. Proc. Natl. Acad. Sci. USA, 2005, 102, 15471-15476.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 15471-15476
    • Kuzmenkina, E.V.1    Heyes, C.D.2    Nienhaus, G.U.3
  • 131
    • 0037195077 scopus 로고    scopus 로고
    • Measurement of microsecond dynamic motion in the intestinal fatty acid bindin g protein by using fluorescence correlation spectroscopy
    • Chattopadhyay, K., Saffarian, S., Elson, E. L. and Frieden, C., Measurement of microsecond dynamic motion in the intestinal fatty acid bindin g protein by using fluorescence correlation spectroscopy. Proc. Natl. Acad. Sci. USA, 2002, 99, 14171-14176.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 14171-14176
    • Chattopadhyay, K.1    Saffarian, S.2    Elson, E.L.3    Frieden, C.4
  • 132
    • 33847254454 scopus 로고    scopus 로고
    • Ultrafast dynamics of protein collapse from single-molecule photon statistics
    • Nettels, D., Gopich, I. V., Hoffmann, A. and Schuler, B., Ultrafast dynamics of protein collapse from single-molecule photon statistics. Proc. Natl. Acad. Sci. USA, 2007, 104, 2655-2660.
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 2655-2660
    • Nettels, D.1    Gopich, I.V.2    Hoffmann, A.3    Schuler, B.4
  • 133
    • 0034773940 scopus 로고    scopus 로고
    • Solvent-induced collapse of alpha-synuclein and acid-denatured cytochrome c
    • Morar, A. S., Olteanu, A., Young, G. B. and Pielak, G. J., Solvent-induced collapse of alpha-synuclein and acid-denatured cytochrome c. Protein Sci., 2001, 10, 2195-2199.
    • (2001) Protein Sci. , vol.10 , pp. 2195-2199
    • Morar, A.S.1    Olteanu, A.2    Young, G.B.3    Pielak, G.J.4
  • 135
    • 0029940033 scopus 로고    scopus 로고
    • Molecular collapse: the rate-limiting step in two-state cytochrome c folding
    • Sosnick, T. R., Mayne, L. and Englander, S. W., Molecular collapse: the rate-limiting step in two-state cytochrome c folding. Proteins, 1996, 24, 413-426.
    • (1996) Proteins , vol.24 , pp. 413-426
    • Sosnick, T.R.1    Mayne, L.2    Englander, S.W.3
  • 137
    • 0031697733 scopus 로고    scopus 로고
    • The burst phase in ribonuclease A folding and solvent dependence of the unfolded state
    • Qi, P. X., Sosnick, T. R. and Englander, S. W., The burst phase in ribonuclease A folding and solvent dependence of the unfolded state. Nature Struct. Biol., 1998, 5, 882-884.
    • (1998) Nature Struct. Biol. , vol.5 , pp. 882-884
    • Qi, P.X.1    Sosnick, T.R.2    Englander, S.W.3
  • 138
    • 0037065672 scopus 로고    scopus 로고
    • Mechanism of formation of a productive molten globule form of barstar
    • Rami, B. R. and Udgaonkar, J. B., Mechanism of formation of a productive molten globule form of barstar. Biochemistry, 2002, 41, 1710-1716.
    • (2002) Biochemistry , vol.41 , pp. 1710-1716
    • Rami, B.R.1    Udgaonkar, J.B.2
  • 139
    • 0142185492 scopus 로고    scopus 로고
    • The denatured state of Engrailed Homeodomain under denaturing and native conditions
    • Mayor, U., Grossmann, J. G., Foster, N. W., Freund, S. M. and Fersht, A. R., The denatured state of Engrailed Homeodomain under denaturing and native conditions. J. Mol. Biol., 2003, 333, 977-991.
    • (2003) J. Mol. Biol. , vol.333 , pp. 977-991
    • Mayor, U.1    Grossmann, J.G.2    Foster, N.W.3    Freund, S.M.4    Fersht, A.R.5
  • 140
    • 27144532135 scopus 로고    scopus 로고
    • Solution structure of a protein denatured state and folding intermediate
    • Religa, T. L., Markson, J. S., Mayor, U., Freund, S. M. and Fersht, A. R., Solution structure of a protein denatured state and folding intermediate. Nature, 2005, 437, 1053-1056.
    • (2005) Nature , vol.437 , pp. 1053-1056
    • Religa, T.L.1    Markson, J.S.2    Mayor, U.3    Freund, S.M.4    Fersht, A.R.5
  • 141
    • 33846817348 scopus 로고    scopus 로고
    • Backbone dynamics of the monomeric l repressor denatured state ensemble under nondenaturing conditions
    • Chugha, P. and Oas, T. G., Backbone dynamics of the monomeric l repressor denatured state ensemble under nondenaturing conditions. Biochemistry, 2007, 46, 1141-1151.
    • (2007) Biochemistry , vol.46 , pp. 1141-1151
    • Chugha, P.1    Oas, T.G.2
  • 142
    • 0028174310 scopus 로고
    • How does a protein fold?
    • Sali, A., Shakhnovich, E. and Karplus, M., How does a protein fold? Nature, 1994, 369, 248-251.
    • (1994) Nature , vol.369 , pp. 248-251
    • Sali, A.1    Shakhnovich, E.2    Karplus, M.3
  • 143
    • 0344301982 scopus 로고    scopus 로고
    • Protein folding: A perspective from theory and experiment
    • Dobson, C. M., Sali, A. and Karplus, M., Protein folding: A perspective from theory and experiment. Angew. Chem. Int. Ed., 1998, 37, 868-893.
    • (1998) Angew. Chem. Int. Ed. , vol.37 , pp. 868-893
    • Dobson, C.M.1    Sali, A.2    Karplus, M.3
  • 144
    • 0026781019 scopus 로고
    • Early steps in cytochrome c folding probed by time-resolved circular dichroism and fluorescence spectroscopy
    • Elove, G. A., Chaffotte, A. F., Roder, H. and Goldberg, M. E., Early steps in cytochrome c folding probed by time-resolved circular dichroism and fluorescence spectroscopy. Biochemistry, 1992, 31, 6876-6883.
    • (1992) Biochemistry , vol.31 , pp. 6876-6883
    • Elove, G.A.1    Chaffotte, A.F.2    Roder, H.3    Goldberg, M.E.4
  • 145
    • 0027749370 scopus 로고
    • Formation of a molten globule intermediate early in the kinetic folding pathway of apomyoglobin
    • Jennings, P. A. and Wright, P. E., Formation of a molten globule intermediate early in the kinetic folding pathway of apomyoglobin. Science, 1993, 262, 892-896.
    • (1993) Science , vol.262 , pp. 892-896
    • Jennings, P.A.1    Wright, P.E.2
  • 146
    • 0029738416 scopus 로고    scopus 로고
    • Circular dichroism evidence for the presence of burst-phase intermediates on the conformational folding pathway of ribonuclease A
    • Houry, W. A., Rothwarf, D. M. and Scheraga, H. A., Circular dichroism evidence for the presence of burst-phase intermediates on the conformational folding pathway of ribonuclease A. Biochemistry, 1996, 35, 10125-10133.
    • (1996) Biochemistry , vol.35 , pp. 10125-10133
    • Houry, W.A.1    Rothwarf, D.M.2    Scheraga, H.A.3
  • 147
    • 0030057477 scopus 로고    scopus 로고
    • Evidence for a three-state model of protein folding from kinetic analysis of ubiquitin variants with altered core residues
    • Khorasanizadeh, S., Peters, I. D. and Roder, H., Evidence for a three-state model of protein folding from kinetic analysis of ubiquitin variants with altered core residues. Nature Struct. Biol., 1996, 3, 193-205.
    • (1996) Nature Struct. Biol. , vol.3 , pp. 193-205
    • Khorasanizadeh, S.1    Peters, I.D.2    Roder, H.3
  • 148
    • 0030664958 scopus 로고    scopus 로고
    • An early intermediate in the folding reaction of the B1 domain of protein G contains a native-like core
    • Park, S. H., O'Neil, K. T. and Roder, H., An early intermediate in the folding reaction of the B1 domain of protein G contains a native-like core. Biochemistry, 1997, 36, 14277-14283.
    • (1997) Biochemistry , vol.36 , pp. 14277-14283
    • Park, S.H.1    O'Neil, K.T.2    Roder, H.3
  • 149
    • 0030961780 scopus 로고    scopus 로고
    • The kinetic folding intermediate of ribonuclease H resembles the acid molten globule and partially unfolded molecules detected under native conditions
    • Raschke, T. M. and Marqusee, S., The kinetic folding intermediate of ribonuclease H resembles the acid molten globule and partially unfolded molecules detected under native conditions. Nature Struct. Biol., 1997, 4, 298-304.
    • (1997) Nature Struct. Biol. , vol.4 , pp. 298-304
    • Raschke, T.M.1    Marqusee, S.2
  • 150
    • 0031055942 scopus 로고    scopus 로고
    • Kinetic role of early intermediates in protein folding
    • Roder, H., Colon, W., Kinetic role of early intermediates in protein folding. Curr. Opin. Struct. Biol., 1997, 7, 15-28.
    • (1997) Curr. Opin. Struct. Biol. , vol.7 , pp. 15-28
    • Roder, H.1    Colon, W.2
  • 151
    • 0028917296 scopus 로고
    • Structures of folding intermediates
    • Ptitsyn, O. B., Structures of folding intermediates. Curr. Opin. Struct. Biol., 1995, 5, 74-78.
    • (1995) Curr. Opin. Struct. Biol. , vol.5 , pp. 74-78
    • Ptitsyn, O.B.1
  • 152
    • 0030059690 scopus 로고    scopus 로고
    • The molten globule state of alpha-lactalbumin
    • Kuwajima, K., The molten globule state of alpha-lactalbumin. FASEB J., 1996, 10, 102-109.
    • (1996) FASEB J. , vol.10 , pp. 102-109
    • Kuwajima, K.1
  • 153
    • 0030348041 scopus 로고    scopus 로고
    • Rapid formation of a molten globule intermediate in refolding of alpha-lactalbumin
    • Arai, M. and Kuwajima, K., Rapid formation of a molten globule intermediate in refolding of alpha-lactalbumin. Fold. Des., 1996, 1, 275-287.
    • (1996) Fold. Des. , vol.1 , pp. 275-287
    • Arai, M.1    Kuwajima, K.2
  • 154
    • 0029115374 scopus 로고
    • Kinetics of interaction of partially folded proteins with a hydrophobic dye: evidence that molten globule character is maximal in early folding intermediates
    • Engelhard, M. and Evans, P. A., Kinetics of interaction of partially folded proteins with a hydrophobic dye: evidence that molten globule character is maximal in early folding intermediates. Protein Sci., 1995, 4, 1553-1562.
    • (1995) Protein Sci. , vol.4 , pp. 1553-1562
    • Engelhard, M.1    Evans, P.A.2
  • 155
    • 0029967474 scopus 로고    scopus 로고
    • Side chain packing of the N and C-terminal helices plays a critical role in the kinetics of cytochrome c folding
    • Colon, W., Elove, G. A., Wakem, L. P., Sherman, F. and Roder, H., Side chain packing of the N and C-terminal helices plays a critical role in the kinetics of cytochrome c folding. Biochemistry, 1996, 35, 5538-5549.
    • (1996) Biochemistry , vol.35 , pp. 5538-5549
    • Colon, W.1    Elove, G.A.2    Wakem, L.P.3    Sherman, F.4    Roder, H.5
  • 156
    • 0034665642 scopus 로고    scopus 로고
    • The slow folding reaction of barstar: the core tryptophan region attains tight packing before substantial secondary and tertiary structure formation and final compaction of the polypeptide chain
    • Sridevi, K., Juneja, J., Bhuyan, A. K., Krishnamoorthy, G. and Udgaonkar, J. B., The slow folding reaction of barstar: the core tryptophan region attains tight packing before substantial secondary and tertiary structure formation and final compaction of the polypeptide chain. J. Mol. Biol., 2000, 302, 479-495.
    • (2000) J. Mol. Biol. , vol.302 , pp. 479-495
    • Sridevi, K.1    Juneja, J.2    Bhuyan, A.K.3    Krishnamoorthy, G.4    Udgaonkar, J.B.5
  • 157
    • 0038047141 scopus 로고    scopus 로고
    • Dynamics of the core tryptophan during the formation of a productive molten globule intermediate of barstar
    • Rami, B. R., Krishnamoorthy, G. and Udgaonkar, J. B., Dynamics of the core tryptophan during the formation of a productive molten globule intermediate of barstar. Biochemistry, 2003, 42, 7986-8000.
    • (2003) Biochemistry , vol.42 , pp. 7986-8000
    • Rami, B.R.1    Krishnamoorthy, G.2    Udgaonkar, J.B.3
  • 158
    • 0036438892 scopus 로고    scopus 로고
    • Differential salt-induced stabilization of structure in the initial folding intermediate ensemble of barstar
    • Pradeep, L. and Udgaonkar, J. B., Differential salt-induced stabilization of structure in the initial folding intermediate ensemble of barstar. J. Mol. Biol., 2002, 324, 331-347.
    • (2002) J. Mol. Biol. , vol.324 , pp. 331-347
    • Pradeep, L.1    Udgaonkar, J.B.2
  • 159
    • 38049108092 scopus 로고    scopus 로고
    • Exploring the cooperativity of the fast folding reaction of a small protein using pulsed thiol labeling and mass spectrometry
    • Jha, S. K. and Udgaonkar, J. B., Exploring the cooperativity of the fast folding reaction of a small protein using pulsed thiol labeling and mass spectrometry. J. Biol. Chem., 2007, 282, 37479-37491.
    • (2007) J. Biol. Chem. , vol.282 , pp. 37479-37491
    • Jha, S.K.1    Udgaonkar, J.B.2
  • 161
    • 0347284262 scopus 로고    scopus 로고
    • Rapid collapse precedes the fast two-state folding of the cold shock protein
    • Magg, C. and Schmid, F. X., Rapid collapse precedes the fast two-state folding of the cold shock protein. J. Mol. Biol., 2004, 335, 1309-1323.
    • (2004) J. Mol. Biol. , vol.335 , pp. 1309-1323
    • Magg, C.1    Schmid, F.X.2
  • 162
    • 33745955427 scopus 로고    scopus 로고
    • Specificity of the initial collapse in the folding of the cold shock protein
    • Magg, C., Kubelka, J., Holtermann, G., Haas, E. and Schmid, F. X., Specificity of the initial collapse in the folding of the cold shock protein. J. Mol. Biol., 2006, 360, 1067-1080.
    • (2006) J. Mol. Biol. , vol.360 , pp. 1067-1080
    • Magg, C.1    Kubelka, J.2    Holtermann, G.3    Haas, E.4    Schmid, F.X.5
  • 163
    • 0033550298 scopus 로고    scopus 로고
    • The cooperativity of burst phase reactions explored
    • Parker, M. J. and Marqusee, S., The cooperativity of burst phase reactions explored. J. Mol. Biol., 1999, 293, 1195-1210.
    • (1999) J. Mol. Biol. , vol.293 , pp. 1195-1210
    • Parker, M.J.1    Marqusee, S.2
  • 164
    • 0032516445 scopus 로고    scopus 로고
    • Proline isomerization-independent accumulation of an early intermediate and heterogeneity of the folding pathways of a mixed alpha/beta protein, Escherichia coli thioredoxin
    • Georgescu, R. E., Li, J. H., Goldberg, M. E., Tasayco, M. L. and Chaffotte, A. F., Proline isomerization-independent accumulation of an early intermediate and heterogeneity of the folding pathways of a mixed alpha/beta protein, Escherichia coli thioredoxin. Biochemistry, 1998, 37, 10286-10297.
    • (1998) Biochemistry , vol.37 , pp. 10286-10297
    • Georgescu, R.E.1    Li, J.H.2    Goldberg, M.E.3    Tasayco, M.L.4    Chaffotte, A.F.5
  • 165
    • 0025849701 scopus 로고
    • Calorimetric determination of the enthalpy change for the alpha-helix to coil transition of an alanine peptide in water
    • Scholtz, J. M., Marqusee, S., Baldwin, R. L., York, E. J., Stewart, J. M., Santoro, M. and Bolen, D. W., Calorimetric determination of the enthalpy change for the alpha-helix to coil transition of an alanine peptide in water. Proc. Natl. Acad. Sci. USA, 1991, 88, 2854-2858.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 2854-2858
    • Scholtz, J.M.1    Marqusee, S.2    Baldwin, R.L.3    York, E.J.4    Stewart, J.M.5    Santoro, M.6    Bolen, D.W.7
  • 167
    • 0030768045 scopus 로고    scopus 로고
    • A residue-specific NMR view of the non-cooperative unfolding of a molten globule
    • Schulman, B. A., Kim, P. S., Dobson, C. M. and Redfield, C., A residue-specific NMR view of the non-cooperative unfolding of a molten globule. Nature Struct. Biol., 1997, 4, 630-634.
    • (1997) Nature Struct. Biol. , vol.4 , pp. 630-634
    • Schulman, B.A.1    Kim, P.S.2    Dobson, C.M.3    Redfield, C.4
  • 168
    • 33846099514 scopus 로고    scopus 로고
    • Mapping protein collapse with single-molecule fluorescence and kinetic synchrotron radiation circular dichroism spectroscopy
    • Hoffmann, A. et al., Mapping protein collapse with single-molecule fluorescence and kinetic synchrotron radiation circular dichroism spectroscopy. Proc. Natl. Acad. Sci. USA, 2007, 104, 105-110.
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 105-110
    • Hoffmann, A.1
  • 169
    • 3242883536 scopus 로고    scopus 로고
    • Rapid mixing methods for exploring the kinetics of protein folding
    • Roder, H., Maki, K., Cheng, H. and Shastry, M. C., Rapid mixing methods for exploring the kinetics of protein folding. Methods, 2004, 34, 15-27.
    • (2004) Methods , vol.34 , pp. 15-27
    • Roder, H.1    Maki, K.2    Cheng, H.3    Shastry, M.C.4
  • 170
  • 171
    • 0037162450 scopus 로고    scopus 로고
    • Early kinetic intermediate in the folding of acyl-CoA binding protein detected by fluorescence labeling and ultrarapid mixing
    • Teilum, K., Maki, K., Kragelund, B. B., Poulsen, F. M. and Roder, H., Early kinetic intermediate in the folding of acyl-CoA binding protein detected by fluorescence labeling and ultrarapid mixing. Proc. Natl. Acad. Sci. USA, 2002, 99, 9807-9812.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 9807-9812
    • Teilum, K.1    Maki, K.2    Kragelund, B.B.3    Poulsen, F.M.4    Roder, H.5
  • 172
    • 33947327195 scopus 로고    scopus 로고
    • Folding kinetics of staphylococcal nuclease studied by tryptophan engineering and rapid mixing methods
    • Maki, K., Cheng, H., Dolgikh, D. A. and Roder, H., Folding kinetics of staphylococcal nuclease studied by tryptophan engineering and rapid mixing methods. J. Mol. Biol., 2007, 368, 244-255.
    • (2007) J. Mol. Biol. , vol.368 , pp. 244-255
    • Maki, K.1    Cheng, H.2    Dolgikh, D.A.3    Roder, H.4
  • 173
    • 0037235662 scopus 로고    scopus 로고
    • Exponential decay kinetics in 'downhill' protein folding
    • Hagen, S. J., Exponential decay kinetics in 'downhill' protein folding. Proteins, 2003, 50, 1-4.
    • (2003) Proteins , vol.50 , pp. 1-4
    • Hagen, S.J.1
  • 174
    • 33749027499 scopus 로고    scopus 로고
    • Criteria for downhill protein folding: calorimetry, chevron plot, kinetic relaxation, and single-molecule radius of gyration in chain models with subdued degrees of cooperativity
    • Knott, M. and Chan, H. S., Criteria for downhill protein folding: calorimetry, chevron plot, kinetic relaxation, and single-molecule radius of gyration in chain models with subdued degrees of cooperativity. Proteins, 2006, 65, 373-391.
    • (2006) Proteins , vol.65 , pp. 373-391
    • Knott, M.1    Chan, H.S.2
  • 175
    • 0032989351 scopus 로고    scopus 로고
    • Observation of strange kinetics in protein folding
    • Sabelko, J., Ervin, J. and Gruebele, M., Observation of strange kinetics in protein folding. Proc. Natl. Acad. Sci. USA, 1999, 96, 6031-6036.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 6031-6036
    • Sabelko, J.1    Ervin, J.2    Gruebele, M.3
  • 176
    • 0042527446 scopus 로고    scopus 로고
    • Highly nonexponential kinetics in the early-phase refolding of proteins at low temperatures
    • Saigo, S. and Shibayama, N., Highly nonexponential kinetics in the early-phase refolding of proteins at low temperatures. Biochemistry, 2003, 42, 9669-9676.
    • (2003) Biochemistry , vol.42 , pp. 9669-9676
    • Saigo, S.1    Shibayama, N.2
  • 177
    • 35548977602 scopus 로고    scopus 로고
    • Temperature-dependent heme kinetics with nonexponential binding and barrier relaxation in the absence of protein conformational substates
    • Ye, X., Ionascu, D., Gruia, F., Yu, A., Benabbas, A. and Champion, P. M., Temperature-dependent heme kinetics with nonexponential binding and barrier relaxation in the absence of protein conformational substates. Proc. Natl. Acad. Sci. USA, 2007, 104, 14682-14687.
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 14682-14687
    • Ye, X.1    Ionascu, D.2    Gruia, F.3    Yu, A.4    Benabbas, A.5    Champion, P.M.6
  • 178
    • 0034714154 scopus 로고    scopus 로고
    • Two-state expansion and collapse of a polypeptide
    • Hagen, S. J. and Eaton, W. A., Two-state expansion and collapse of a polypeptide. J. Mol. Biol., 2000, 301, 1019-1027.
    • (2000) J. Mol. Biol. , vol.301 , pp. 1019-1027
    • Hagen, S.J.1    Eaton, W.A.2
  • 179
    • 0037667601 scopus 로고    scopus 로고
    • Fast chain contraction during protein folding: 'foldability' and collapse dynamics
    • Qiu, L., Zachariah, C. and Hagen, S. J., Fast chain contraction during protein folding: 'foldability' and collapse dynamics. Phys. Rev. Lett., 2003, 90, 168103.
    • (2003) Phys. Rev. Lett. , vol.90 , pp. 168103
    • Qiu, L.1    Zachariah, C.2    Hagen, S.J.3
  • 180
    • 0842299585 scopus 로고    scopus 로고
    • Collapse and search dynamics of apomyoglobin folding revealed by submillisecond observations of alpha-helical content and compactness
    • Uzawa, T., Akiyama, S., Kimura, T., Takahashi, S., Ishimori, K., Morishima, I. and Fujisawa, T., Collapse and search dynamics of apomyoglobin folding revealed by submillisecond observations of alpha-helical content and compactness. Proc. Natl. Acad. Sci. USA, 2004, 101, 1171-1176.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 1171-1176
    • Uzawa, T.1    Akiyama, S.2    Kimura, T.3    Takahashi, S.4    Ishimori, K.5    Morishima, I.6    Fujisawa, T.7
  • 182
    • 32344442512 scopus 로고    scopus 로고
    • Molecular dimensions and their distributions in early folding intermediates
    • Bilsel, O. and Matthews, C. R., Molecular dimensions and their distributions in early folding intermediates. Curr. Opin. Struct. Biol., 2006, 16, 86-93.
    • (2006) Curr. Opin. Struct. Biol. , vol.16 , pp. 86-93
    • Bilsel, O.1    Matthews, C.R.2
  • 184
    • 33846041173 scopus 로고    scopus 로고
    • Sitespecific collapse dynamics guide the formation of the cytochrome c′ four-helix bundle
    • Kimura, T., Lee, J. C., Gray, H. B. and Winkler, J. R., Sitespecific collapse dynamics guide the formation of the cytochrome c′ four-helix bundle. Proc. Natl. Acad. Sci. USA, 2007, 104, 117-122.
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 117-122
    • Kimura, T.1    Lee, J.C.2    Gray, H.B.3    Winkler, J.R.4
  • 185
    • 0001631778 scopus 로고
    • Rate processes with dynamical disorder
    • Zwanzig, R., Rate processes with dynamical disorder. Acc. Chem. Res., 1990, 23, 148-152.
    • (1990) Acc. Chem. Res. , vol.23 , pp. 148-152
    • Zwanzig, R.1
  • 186
    • 0037225280 scopus 로고    scopus 로고
    • Evidence for sequential barriers and obligatory intermediates in apparent two-state protein folding
    • Sanchez, I. E. and Kiefhaber, T., Evidence for sequential barriers and obligatory intermediates in apparent two-state protein folding. J. Mol. Biol., 2003, 325, 367-376.
    • (2003) J. Mol. Biol. , vol.325 , pp. 367-376
    • Sanchez, I.E.1    Kiefhaber, T.2
  • 187
    • 0025133511 scopus 로고
    • Early folding intermediate of ribonuclease A
    • Udgaonkar, J. B. and Baldwin, R. L., Early folding intermediate of ribonuclease A. Proc. Natl. Acad. Sci. USA, 1990, 87, 8197-8201.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 8197-8201
    • Udgaonkar, J.B.1    Baldwin, R.L.2
  • 188
    • 0029811091 scopus 로고    scopus 로고
    • Structure of a hydrophobically collapsed intermediate on the conformational folding pathway of ribonuclease A probed by hydrogen-deuterium exchange
    • Houry, W. A. and Scheraga, H. A., Structure of a hydrophobically collapsed intermediate on the conformational folding pathway of ribonuclease A probed by hydrogen-deuterium exchange. Biochemistry, 1996, 35, 11734-11746.
    • (1996) Biochemistry , vol.35 , pp. 11734-11746
    • Houry, W.A.1    Scheraga, H.A.2
  • 189
    • 0030334648 scopus 로고    scopus 로고
    • An evaluation of the use of hydrogen exchange at equilibrium to probe intermediates on the protein folding pathway
    • Clarke, J. and Fersht, A. R., An evaluation of the use of hydrogen exchange at equilibrium to probe intermediates on the protein folding pathway. Fold. Des., 1996, 1, 243-254.
    • (1996) Fold. Des. , vol.1 , pp. 243-254
    • Clarke, J.1    Fersht, A.R.2
  • 191
    • 0031932824 scopus 로고    scopus 로고
    • Structural and dynamic characterization of partially folded states of apomyoglobin and implications for protein folding
    • Eliezer, D., Yao, J., Dyson, H. J. and Wright, P. E., Structural and dynamic characterization of partially folded states of apomyoglobin and implications for protein folding. Nature Struct. Biol., 1998, 5, 148-155.
    • (1998) Nature Struct. Biol. , vol.5 , pp. 148-155
    • Eliezer, D.1    Yao, J.2    Dyson, H.J.3    Wright, P.E.4
  • 193
    • 0025150383 scopus 로고
    • Origins of structure in globular proteins
    • Chan, H. S. and Dill, K. A., Origins of structure in globular proteins. Proc. Natl. Acad. Sci. USA, 1990, 87, 6388-6392.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 6388-6392
    • Chan, H.S.1    Dill, K.A.2
  • 194
    • 0035179018 scopus 로고    scopus 로고
    • Helics nucleation kinetics from molecular simulations in explicit solvent
    • Hummer, G., Garcia, A. E. and Garde, S., Helics nucleation kinetics from molecular simulations in explicit solvent. Proteins, 2001, 42, 77-84.
    • (2001) Proteins , vol.42 , pp. 77-84
    • Hummer, G.1    Garcia, A.E.2    Garde, S.3
  • 195
    • 14544272814 scopus 로고    scopus 로고
    • Specific collapse followed by slow hydrogenbond formation of beta-sheet in the folding of single-chain monellin
    • Kimura, T. et al., Specific collapse followed by slow hydrogenbond formation of beta-sheet in the folding of single-chain monellin. Proc. Natl. Acad. Sci. USA, 2005, 102, 2748-2753.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 2748-2753
    • Kimura, T.1
  • 196
    • 51649090393 scopus 로고    scopus 로고
    • Dehydration of main-chain amides in the final folding step of single-chain monellin revealed by time-resolved infrared spectroscopy
    • Kimura, T. et al., Dehydration of main-chain amides in the final folding step of single-chain monellin revealed by time-resolved infrared spectroscopy. Proc. Natl. Acad. Sci. USA, 2008, 105, 13391-13396.
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 13391-13396
    • Kimura, T.1
  • 197
    • 33644554831 scopus 로고    scopus 로고
    • Role of unfolded state heterogeneity and en-route ruggedness in protein folding kinetics
    • Ellison, P. A. and Cavagnero, S., Role of unfolded state heterogeneity and en-route ruggedness in protein folding kinetics. Protein Sci., 2006, 15, 564-582.
    • (2006) Protein Sci. , vol.15 , pp. 564-582
    • Ellison, P.A.1    Cavagnero, S.2
  • 198
    • 0032561237 scopus 로고    scopus 로고
    • Pathways to a protein folding intermediate observed in a 1-microsecond simulation in aqueous solution
    • Duan, Y. and Kollman, P. A., Pathways to a protein folding intermediate observed in a 1-microsecond simulation in aqueous solution. Science, 1998, 282, 740-744.
    • (1998) Science , vol.282 , pp. 740-744
    • Duan, Y.1    Kollman, P.A.2
  • 199
    • 33745931359 scopus 로고    scopus 로고
    • Multiple routes lead to the native state in the energy landscape of the beta-trefoil family
    • Chavez, L. L., Gosavi, S., Jennings, P. A. and Onuchic, J. N., Multiple routes lead to the native state in the energy landscape of the beta-trefoil family. Proc. Natl. Acad. Sci. USA, 2006, 103, 10254-10258.
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 10254-10258
    • Chavez, L.L.1    Gosavi, S.2    Jennings, P.A.3    Onuchic, J.N.4
  • 200
    • 0026751786 scopus 로고
    • The folding of hen lysozyme involves partially structured intermediates and multiple pathways
    • Radford, S. E., Dobson, C. M. and Evans, P. A., The folding of hen lysozyme involves partially structured intermediates and multiple pathways. Nature, 1992, 358, 302-307.
    • (1992) Nature , vol.358 , pp. 302-307
    • Radford, S.E.1    Dobson, C.M.2    Evans, P.A.3
  • 201
    • 0029760326 scopus 로고    scopus 로고
    • Different folding transition states may result in the same native structure
    • Viguera, A. R., Serrano, L. and Wilmanns, M., Different folding transition states may result in the same native structure. Nature Struct. Biol., 1996, 3, 874-880.
    • (1996) Nature Struct. Biol. , vol.3 , pp. 874-880
    • Viguera, A.R.1    Serrano, L.2    Wilmanns, M.3
  • 202
    • 0036829967 scopus 로고    scopus 로고
    • Complete change of the protein folding transition state upon circular permutation
    • Lindberg, M. O., Tangrot, J. and Oliveberg, M., Complete change of the protein folding transition state upon circular permutation. Nature Struct. Biol., 2002, 9, 818-822.
    • (2002) Nature Struct. Biol. , vol.9 , pp. 818-822
    • Lindberg, M.O.1    Tangrot, J.2    Oliveberg, M.3
  • 203
    • 51649106422 scopus 로고    scopus 로고
    • Microsecond acquisition of heterogeneous structure in the folding of a TIM barrel protein
    • Wu, Y., Kondrashkina, E., Kayatekin, C., Matthews, C. R. and Bilsel, O., Microsecond acquisition of heterogeneous structure in the folding of a TIM barrel protein. Proc. Natl. Acad. Sci. USA, 2008, 105, 13367-13372.
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 13367-13372
    • Wu, Y.1    Kondrashkina, E.2    Kayatekin, C.3    Matthews, C.R.4    Bilsel, O.5
  • 204
    • 34047194846 scopus 로고    scopus 로고
    • Conformational equilibration time of unfolded protein chains and the folding speed limit
    • Abel, C. J., Goldbeck, R. A., Latypov, R. F., Roder, H. and Kliger, D. S., Conformational equilibration time of unfolded protein chains and the folding speed limit. Biochemistry, 2007, 46, 4090-4099.
    • (2007) Biochemistry , vol.46 , pp. 4090-4099
    • Abel, C.J.1    Goldbeck, R.A.2    Latypov, R.F.3    Roder, H.4    Kliger, D.S.5
  • 205
    • 33846438226 scopus 로고    scopus 로고
    • End-to-end vs interior loop formation kinetics in unfolded polypeptide chains
    • Fierz, B. and Kiefhaber, T., End-to-end vs interior loop formation kinetics in unfolded polypeptide chains. J. Am. Chem. Soc., 2007, 129, 672-679.
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 672-679
    • Fierz, B.1    Kiefhaber, T.2
  • 206
    • 0031890195 scopus 로고    scopus 로고
    • Conservation of rapid two-state folding in mesophilic, thermophilic and hyperthermophilic cold shock proteins
    • Perl, D., Welker, C., Schindler, T., Schroder, K., Marahiel, M. A., Jaenicke, R. and Schmid, F. X., Conservation of rapid two-state folding in mesophilic, thermophilic and hyperthermophilic cold shock proteins. Nature Struct. Biol., 1998, 5, 229-235.
    • (1998) Nature Struct. Biol. , vol.5 , pp. 229-235
    • Perl, D.1    Welker, C.2    Schindler, T.3    Schroder, K.4    Marahiel, M.A.5    Jaenicke, R.6    Schmid, F.X.7
  • 208
    • 0030450051 scopus 로고    scopus 로고
    • Thermodynamic properties of an extremely rapid protein folding reaction
    • Schindler, T. and Schmid, F. X., Thermodynamic properties of an extremely rapid protein folding reaction. Biochemistry, 1996, 35, 16833-16842.
    • (1996) Biochemistry , vol.35 , pp. 16833-16842
    • Schindler, T.1    Schmid, F.X.2
  • 209
    • 0037456298 scopus 로고    scopus 로고
    • The complete folding pathway of a protein from nanoseconds to microseconds
    • Mayor, U. et al., The complete folding pathway of a protein from nanoseconds to microseconds. Nature, 2003, 421, 863-867.
    • (2003) Nature , vol.421 , pp. 863-867
    • Mayor, U.1
  • 210
    • 0037032225 scopus 로고    scopus 로고
    • Smaller and faster: the 20-residue Trp-cage protein folds in 4 micros
    • Qiu, L., Pabit, S. A., Roitberg, A. E. and Hagen, S. J., Smaller and faster: the 20-residue Trp-cage protein folds in 4 micros. J. Am. Chem. Soc., 2002, 124, 12952-12953.
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 12952-12953
    • Qiu, L.1    Pabit, S.A.2    Roitberg, A.E.3    Hagen, S.J.4
  • 211
    • 3142782241 scopus 로고    scopus 로고
    • Quantifying the roughness on the free energy landscape: entropic bottlenecks and protein folding rates
    • Chavez, L. L., Onuchic, J. N. and Clementi, C., Quantifying the roughness on the free energy landscape: entropic bottlenecks and protein folding rates. J. Am. Chem. Soc., 2004, 126, 8426-8432.
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 8426-8432
    • Chavez, L.L.1    Onuchic, J.N.2    Clementi, C.3
  • 212
    • 0032502839 scopus 로고    scopus 로고
    • Contact order, transition state placement and the refolding rates of single domain proteins
    • Plaxco, K. W., Simons, K. T. and Baker, D., Contact order, transition state placement and the refolding rates of single domain proteins. J. Mol. Biol., 1998, 277, 985-994.
    • (1998) J. Mol. Biol. , vol.277 , pp. 985-994
    • Plaxco, K.W.1    Simons, K.T.2    Baker, D.3
  • 213
    • 0034604105 scopus 로고    scopus 로고
    • A surprising simplicity to protein folding
    • Baker, D., A surprising simplicity to protein folding. Nature, 2000, 405, 39-42.
    • (2000) Nature , vol.405 , pp. 39-42
    • Baker, D.1
  • 214
    • 3943113660 scopus 로고    scopus 로고
    • Using protein folding rates to test protein folding theories
    • Gillespie, B. and Plaxco, K. W., Using protein folding rates to test protein folding theories. Annu. Rev. Biochem., 2004, 73, 837-859.
    • (2004) Annu. Rev. Biochem. , vol.73 , pp. 837-859
    • Gillespie, B.1    Plaxco, K.W.2
  • 215
    • 2542494929 scopus 로고    scopus 로고
    • Unification of the folding mechanisms of non-two-state and two-state proteins
    • Kamagata, K., Arai, M. and Kuwajima, K., Unification of the folding mechanisms of non-two-state and two-state proteins. J. Mol. Biol., 2004, 339, 951-965.
    • (2004) J. Mol. Biol. , vol.339 , pp. 951-965
    • Kamagata, K.1    Arai, M.2    Kuwajima, K.3
  • 216
    • 33645049047 scopus 로고    scopus 로고
    • Surprisingly high correlation between early and late stages in non-two-state protein folding
    • Kamagata, K. and Kuwajima, K., Surprisingly high correlation between early and late stages in non-two-state protein folding. J. Mol. Biol., 2006, 357, 1647-1654.
    • (2006) J. Mol. Biol. , vol.357 , pp. 1647-1654
    • Kamagata, K.1    Kuwajima, K.2
  • 218
    • 33644954340 scopus 로고    scopus 로고
    • Time-resolved small-angle X-ray scattering investigation of the folding dynamics of heme oxygenase: implication of the scaling relationship for the submillisecond intermediates of protein folding
    • Uzawa, T. et al., Time-resolved small-angle X-ray scattering investigation of the folding dynamics of heme oxygenase: implication of the scaling relationship for the submillisecond intermediates of protein folding. J. Mol. Biol., 2006, 357, 997-1008.
    • (2006) J. Mol. Biol. , vol.357 , pp. 997-1008
    • Uzawa, T.1
  • 219
    • 0029973119 scopus 로고    scopus 로고
    • Direct observation of fast protein folding: the initial collapse of apomyoglobin
    • Ballew, R. M., Sabelko, J. and Gruebele, M., Direct observation of fast protein folding: the initial collapse of apomyoglobin. Proc. Natl. Acad. Sci. USA, 1996, 93, 5759-5764.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 5759-5764
    • Ballew, R.M.1    Sabelko, J.2    Gruebele, M.3
  • 221
    • 0003166498 scopus 로고    scopus 로고
    • Protein folding in the landscape perspective: chevron plots and non-Arrhenius kinetics
    • Chan, H. S. and Dill, K. A., Protein folding in the landscape perspective: chevron plots and non-Arrhenius kinetics. Proteins, 1998, 30, 2-33.
    • (1998) Proteins , vol.30 , pp. 2-33
    • Chan, H.S.1    Dill, K.A.2


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