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Volumn 340, Issue 3, 2006, Pages 976-983

Energy barriers, cooperativity, and hidden intermediates in the folding of small proteins

Author keywords

Cooperative stabilization; Energy landscape; Folding intermediates; Kinetic barrier; Transition state

Indexed keywords

PROTEIN;

EID: 30144440755     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2005.12.093     Document Type: Article
Times cited : (27)

References (42)
  • 1
    • 0031815749 scopus 로고    scopus 로고
    • How do small single-domain proteins fold?
    • S.E. Jackson How do small single-domain proteins fold? Fold. Des. 3 1998 R81 R91
    • (1998) Fold. Des. , vol.3
    • Jackson, S.E.1
  • 2
    • 0036440985 scopus 로고    scopus 로고
    • Fast and slow intermediate accumulation and the initial barrier mechanism in protein folding
    • B.A. Krantz, L. Mayne, J. Rumbley, S.W. Englander, and T.R. Sosnick Fast and slow intermediate accumulation and the initial barrier mechanism in protein folding J. Mol. Biol. 324 2002 1 13
    • (2002) J. Mol. Biol. , vol.324 , pp. 1-13
    • Krantz, B.A.1    Mayne, L.2    Rumbley, J.3    Englander, S.W.4    Sosnick, T.R.5
  • 3
    • 0026345750 scopus 로고
    • Folding of chymotrypsin inhibitor 2. 1. Evidence for a two-state transition
    • S.E. Jackson, and A.R. Fersht Folding of chymotrypsin inhibitor 2. 1. Evidence for a two-state transition Biochemistry 30 1991 10428 10435
    • (1991) Biochemistry , vol.30 , pp. 10428-10435
    • Jackson, S.E.1    Fersht, A.R.2
  • 4
    • 0026342150 scopus 로고
    • Folding of chymotrypsin inhibitor 2. 2. Influence of proline isomerization on the folding kinetics and thermodynamic characterization of the transition state of folding
    • S.E. Jackson, and A.R. Fersht Folding of chymotrypsin inhibitor 2. 2. Influence of proline isomerization on the folding kinetics and thermodynamic characterization of the transition state of folding Biochemistry 30 1991 10436 10443
    • (1991) Biochemistry , vol.30 , pp. 10436-10443
    • Jackson, S.E.1    Fersht, A.R.2
  • 5
    • 0029865938 scopus 로고    scopus 로고
    • Future directions in folding: The multi-state nature of protein structure
    • Y. Bai, and S.W. Englander Future directions in folding: the multi-state nature of protein structure Proteins 24 1996 145 151
    • (1996) Proteins , vol.24 , pp. 145-151
    • Bai, Y.1    Englander, S.W.2
  • 6
    • 0029643523 scopus 로고
    • Protein folding intermediates: Native-state hydrogen exchange
    • Y. Bai, T.R. Sosnick, L. Mayne, and S.W. Englander Protein folding intermediates: native-state hydrogen exchange Science 269 1995 192 197
    • (1995) Science , vol.269 , pp. 192-197
    • Bai, Y.1    Sosnick, T.R.2    Mayne, L.3    Englander, S.W.4
  • 7
    • 0037172787 scopus 로고    scopus 로고
    • Relationship between the native-state hydrogen exchange and folding pathways of a four-helix bundle protein
    • R.A. Chu, W.H. Pei, J. Takei, and Y. Bai Relationship between the native-state hydrogen exchange and folding pathways of a four-helix bundle protein Biochemistry 41 2002 7998 8003
    • (2002) Biochemistry , vol.41 , pp. 7998-8003
    • Chu, R.A.1    Pei, W.H.2    Takei, J.3    Bai, Y.4
  • 8
    • 6344291152 scopus 로고    scopus 로고
    • 562: Native fold with non-native hydrophobic interactions
    • 562: native fold with non-native hydrophobic interactions J. Mol. Biol. 343 2004 1477 1485
    • (2004) J. Mol. Biol. , vol.343 , pp. 1477-1485
    • Feng, H.1    Vu, D.2    Bai, Y.3
  • 9
    • 0034687686 scopus 로고    scopus 로고
    • A kinetically significant intermediate in the folding of barnase
    • A.R. Fersht A kinetically significant intermediate in the folding of barnase Proc. Natl. Acad. Sci. USA 97 2000 14121 14126
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 14121-14126
    • Fersht, A.R.1
  • 10
    • 1642307617 scopus 로고    scopus 로고
    • The folding pathway of barnase: The rate-limiting transition state and a hidden intermediate under native conditions
    • N.D. Vu, H. Feng, and Y. Bai The folding pathway of barnase: the rate-limiting transition state and a hidden intermediate under native conditions Biochemistry 2004
    • (2004) Biochemistry
    • Vu, N.D.1    Feng, H.2    Bai, Y.3
  • 11
    • 0037108164 scopus 로고    scopus 로고
    • Populating partially unfolded forms by hydrogen exchange-directed protein engineering
    • J. Takei, W. Pei, D. Vu, and Y. Bai Populating partially unfolded forms by hydrogen exchange-directed protein engineering Biochemistry 41 2002 12308 12312
    • (2002) Biochemistry , vol.41 , pp. 12308-12312
    • Takei, J.1    Pei, W.2    Vu, D.3    Bai, Y.4
  • 12
    • 0242318402 scopus 로고    scopus 로고
    • Specific non-native hydrophobic interactions in a hidden intermediate: Implications for protien folding
    • H. Feng, J. Takei, R. Lipsitz, N. Tjandra, and Y. Bai Specific non-native hydrophobic interactions in a hidden intermediate: implications for protien folding Biochemistry 42 2003 12461 12465
    • (2003) Biochemistry , vol.42 , pp. 12461-12465
    • Feng, H.1    Takei, J.2    Lipsitz, R.3    Tjandra, N.4    Bai, Y.5
  • 13
    • 17044438189 scopus 로고    scopus 로고
    • Protein folding pathway: Multiple folding intermediates at atomic resolution
    • H.Q. Feng, Z. Zhou, and Y. Bai Protein folding pathway: multiple folding intermediates at atomic resolution Proc. Natl. Acad. Sci. USA 102 2005 5026 5031
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 5026-5031
    • Feng, H.Q.1    Zhou, Z.2    Bai, Y.3
  • 14
    • 24644435356 scopus 로고    scopus 로고
    • 562 characterized by protein engineering
    • 562 characterized by protein engineering J. Mol. Biol. 352 2005 757 764
    • (2005) J. Mol. Biol. , vol.352 , pp. 757-764
    • Zhou, Z.1    Huang, Y.2    Bai, Y.3
  • 15
    • 1542319916 scopus 로고    scopus 로고
    • Cooperativity principles in protein folding
    • H.S. Chan, S. Shimizu, and H. Kaya Cooperativity principles in protein folding Methods Enzymol. 380 2004 350 379
    • (2004) Methods Enzymol. , vol.380 , pp. 350-379
    • Chan, H.S.1    Shimizu, S.2    Kaya, H.3
  • 17
    • 0034284060 scopus 로고    scopus 로고
    • Polymer principles of protein calorimetric two-state cooperativity
    • H. Kaya, and H.S. Chan Polymer principles of protein calorimetric two-state cooperativity Proteins 40 2000 637 661
    • (2000) Proteins , vol.40 , pp. 637-661
    • Kaya, H.1    Chan, H.S.2
  • 18
    • 0042130544 scopus 로고    scopus 로고
    • Simple two-state protein folding kinetics requires near-Levinthal thermodynamic cooperativity
    • H. Kaya, and H.S. Chan Simple two-state protein folding kinetics requires near-Levinthal thermodynamic cooperativity Proteins 52 2003 510 523
    • (2003) Proteins , vol.52 , pp. 510-523
    • Kaya, H.1    Chan, H.S.2
  • 19
    • 0032503027 scopus 로고    scopus 로고
    • The changing nature of the protein folding transition state: Implications for the shape of the free-energy profile for folding
    • M. Oliverberg, Y.-J. Tan, M. Silow, and A.R. Fersht The changing nature of the protein folding transition state: implications for the shape of the free-energy profile for folding J. Mol. Biol. 277 1998 933 943
    • (1998) J. Mol. Biol. , vol.277 , pp. 933-943
    • Oliverberg, M.1    Tan, Y.-J.2    Silow, M.3    Fersht, A.R.4
  • 20
    • 0037225280 scopus 로고    scopus 로고
    • Evidence for sequential barrier and obligatory intermediates in apparent two-state protein folding
    • I.E. Sanchez, and T. Kiefhaber Evidence for sequential barrier and obligatory intermediates in apparent two-state protein folding J. Mol. Biol. 325 2003 367 376
    • (2003) J. Mol. Biol. , vol.325 , pp. 367-376
    • Sanchez, I.E.1    Kiefhaber, T.2
  • 21
    • 1642307617 scopus 로고    scopus 로고
    • The folding pathway of barnase: The rate-limiting transition state and a hidden intermediate under native conditions
    • D. Vu, H. Feng, and Y. Bai The folding pathway of barnase: the rate-limiting transition state and a hidden intermediate under native conditions Biochemistry 42 2004 3346 3356
    • (2004) Biochemistry , vol.42 , pp. 3346-3356
    • Vu, D.1    Feng, H.2    Bai, Y.3
  • 22
    • 0031052147 scopus 로고    scopus 로고
    • A desolvation barrier to hydrophobic cluster formation may contribute to the rate-limiting step in protein folding
    • J.A. Rank, and D. Baker A desolvation barrier to hydrophobic cluster formation may contribute to the rate-limiting step in protein folding Protein Sci. 6 1997 347 354
    • (1997) Protein Sci. , vol.6 , pp. 347-354
    • Rank, J.A.1    Baker, D.2
  • 23
    • 19444384541 scopus 로고    scopus 로고
    • Desolvation is a likely origin of robust enthalpic barriers to protein folding
    • Z. Liu, and H.S. Chan Desolvation is a likely origin of robust enthalpic barriers to protein folding J. Mol. Biol. 349 2005 872 889
    • (2005) J. Mol. Biol. , vol.349 , pp. 872-889
    • Liu, Z.1    Chan, H.S.2
  • 25
    • 12344311123 scopus 로고    scopus 로고
    • Detection of a hidden intermediate in the folding of the third domain of PDZ
    • H. Feng, N.D. Vu, and Y. Bai Detection of a hidden intermediate in the folding of the third domain of PDZ J. Mol. Biol. 346 2005 346 352
    • (2005) J. Mol. Biol. , vol.346 , pp. 346-352
    • Feng, H.1    Vu, N.D.2    Bai, Y.3
  • 27
    • 0028882223 scopus 로고
    • Simple model of protein folding kinetics
    • R. Zwanzig Simple model of protein folding kinetics Proc. Natl. Acad. Sci. USA 92 1995 9801 9804
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 9801-9804
    • Zwanzig, R.1
  • 28
    • 0030733858 scopus 로고    scopus 로고
    • Local interactions and the optimization of protein folding
    • R. Doyle, K. Simons, H. Qian, and D. Baker Local interactions and the optimization of protein folding Proteins 29 1997 282 291
    • (1997) Proteins , vol.29 , pp. 282-291
    • Doyle, R.1    Simons, K.2    Qian, H.3    Baker, D.4
  • 29
    • 0032502839 scopus 로고    scopus 로고
    • Contact order, transition state placement and the refolding rates of single domain proteins
    • K.W. Plaxco, K.T. Simons, and D. Baker Contact order, transition state placement and the refolding rates of single domain proteins J. Mol. Biol. 277 1998 985 994
    • (1998) J. Mol. Biol. , vol.277 , pp. 985-994
    • Plaxco, K.W.1    Simons, K.T.2    Baker, D.3
  • 30
    • 0003166498 scopus 로고    scopus 로고
    • Protein folding in the landscape perspective: Chevron plots and non-Arrhenius kinetics
    • H.S. Chan, and K.A. Dill Protein folding in the landscape perspective: chevron plots and non-Arrhenius kinetics Proteins 30 1998 2 33
    • (1998) Proteins , vol.30 , pp. 2-33
    • Chan, H.S.1    Dill, K.A.2
  • 31
    • 0029940033 scopus 로고    scopus 로고
    • Molecular collapse: The rate-limiting step in two-state cytochrome c folding
    • T.R. Sosnick, L. Mayne, and S.W. Englander Molecular collapse: the rate-limiting step in two-state cytochrome c folding Proteins 24 1996 413 426
    • (1996) Proteins , vol.24 , pp. 413-426
    • Sosnick, T.R.1    Mayne, L.2    Englander, S.W.3
  • 33
    • 0002006297 scopus 로고
    • Are there pathways for protein folding?
    • C. Levinthal Are there pathways for protein folding? J. Chim. Phys. 65 1968 44 45
    • (1968) J. Chim. Phys. , vol.65 , pp. 44-45
    • Levinthal, C.1
  • 34
    • 0015597839 scopus 로고
    • Nulceation, rapid folding, and globular intrachain regions in proteins
    • D.B. Wetlaufer Nulceation, rapid folding, and globular intrachain regions in proteins Proc. Natl. Acad. Sci. USA 70 1973 697 701
    • (1973) Proc. Natl. Acad. Sci. USA , vol.70 , pp. 697-701
    • Wetlaufer, D.B.1
  • 35
    • 19444381093 scopus 로고    scopus 로고
    • Chevron behavior and isostable enthalpic barriers in protein folding: Successes and limitations of Go-like modeling
    • H. Kaya, Z. Liu, and H.S. Chan Chevron behavior and isostable enthalpic barriers in protein folding: successes and limitations of Go-like modeling Biophys. J. 89 2005 520 535
    • (2005) Biophys. J. , vol.89 , pp. 520-535
    • Kaya, H.1    Liu, Z.2    Chan, H.S.3
  • 37
    • 0032502803 scopus 로고    scopus 로고
    • Molecular mechanisms for cooperative folding of proteins
    • M.H. Hao, and H.A. Scheraga Molecular mechanisms for cooperative folding of proteins J. Mol. Biol. 277 1998 973 983
    • (1998) J. Mol. Biol. , vol.277 , pp. 973-983
    • Hao, M.H.1    Scheraga, H.A.2
  • 38
    • 0029809182 scopus 로고    scopus 로고
    • On the origin of the cooperativity of protein folding: Implications from model simulations
    • A. Kolinski, W. Galazka, and J. Skolnick On the origin of the cooperativity of protein folding: implications from model simulations Proteins 26 1996 271 287
    • (1996) Proteins , vol.26 , pp. 271-287
    • Kolinski, A.1    Galazka, W.2    Skolnick, J.3
  • 39
    • 1842635571 scopus 로고    scopus 로고
    • Characterization of the folding energy landscapes of computer generated proteins suggests high folding free enrgy barriers and cooperativity may be consequences of natural selection
    • M. Scalley-Kim, and D. Baker Characterization of the folding energy landscapes of computer generated proteins suggests high folding free enrgy barriers and cooperativity may be consequences of natural selection J. Mol. Biol. 338 2004 573 583
    • (2004) J. Mol. Biol. , vol.338 , pp. 573-583
    • Scalley-Kim, M.1    Baker, D.2
  • 40
    • 2342528494 scopus 로고    scopus 로고
    • Selection of stably folded proteins by phage-display with proteolysis
    • Y. Bai, and H. Feng Selection of stably folded proteins by phage-display with proteolysis Eur. J. Biochem. 271 2004 1609 1614
    • (2004) Eur. J. Biochem. , vol.271 , pp. 1609-1614
    • Bai, Y.1    Feng, H.2
  • 41
    • 0023449962 scopus 로고
    • Spin glasses and the statistical mechanics of protein folding
    • J.D. Bryngelson, and P.G. Wolynes Spin glasses and the statistical mechanics of protein folding Proc. Natl. Acad. Sci. USA 84 1987 7524 7528
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 7524-7528
    • Bryngelson, J.D.1    Wolynes, P.G.2
  • 42
    • 0034710944 scopus 로고    scopus 로고
    • Nonglassy kinetics in the folding of a simple single-domain protein
    • B. Gillespie, and K.W. Plaxco Nonglassy kinetics in the folding of a simple single-domain protein Proc. Natl. Acad. Sci. USA 97 2000 12014 12019
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 12014-12019
    • Gillespie, B.1    Plaxco, K.W.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.