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Volumn 13, Issue 7, 2005, Pages 1047-1054

Scaling behavior and structure of denatured proteins

Author keywords

[No Author keywords available]

Indexed keywords

CHAPERONIN; CREATINE KINASE; GLYCINE CLEAVAGE SYSTEM; LYSOZYME; MYOGLOBIN; PROTEIN; PROTEIN G; PROTEIN KINASE FYN; RIBONUCLEASE A; UBIQUITIN;

EID: 21744448828     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.str.2005.04.009     Document Type: Article
Times cited : (57)

References (34)
  • 1
    • 0027250665 scopus 로고
    • Primary structure effects on peptide group hydrogen exchange
    • Y. Bai, J.S. Milne, L. Mayne, and S.W. Englander Primary structure effects on peptide group hydrogen exchange Proteins 17 1993 75 86
    • (1993) Proteins , vol.17 , pp. 75-86
    • Bai, Y.1    Milne, J.S.2    Mayne, L.3    Englander, S.W.4
  • 2
    • 0033080081 scopus 로고    scopus 로고
    • Is protein folding hierarchic? II. Folding intermediates and transition states
    • R.L. Baldwin, and G.D. Rose Is protein folding hierarchic? II. Folding intermediates and transition states Trends Biochem. Sci. 24 1999 77 83
    • (1999) Trends Biochem. Sci. , vol.24 , pp. 77-83
    • Baldwin, R.L.1    Rose, G.D.2
  • 5
  • 8
    • 0035965129 scopus 로고    scopus 로고
    • Dynamic regimes and correlated structural dynamics in native and denatured alpha-lactalbumin
    • Z. Bu, J. Cook, and D.J. Callaway Dynamic regimes and correlated structural dynamics in native and denatured alpha-lactalbumin J. Mol. Biol. 312 2001 865 873
    • (2001) J. Mol. Biol. , vol.312 , pp. 865-873
    • Bu, Z.1    Cook, J.2    Callaway, D.J.3
  • 9
    • 0034685604 scopus 로고    scopus 로고
    • Topological and energetic factors: What determines the structural details of the transition state ensemble and "en-route" intermediates for protein folding? An investigation for small globular proteins
    • C. Clementi, H. Nymeyer, and J.N. Onuchic Topological and energetic factors: what determines the structural details of the transition state ensemble and "en-route" intermediates for protein folding? An investigation for small globular proteins J. Mol. Biol. 298 2000 937 953
    • (2000) J. Mol. Biol. , vol.298 , pp. 937-953
    • Clementi, C.1    Nymeyer, H.2    Onuchic, J.N.3
  • 11
    • 0036927818 scopus 로고    scopus 로고
    • Direct molecular dynamics observation of protein folding transition state ensemble
    • F. Ding, N.V. Dokholyan, S.V. Buldyrev, H.E. Stanley, and E.I. Shakhnovich Direct molecular dynamics observation of protein folding transition state ensemble Biophys. J. 83 2002 3525 3532
    • (2002) Biophys. J. , vol.83 , pp. 3525-3532
    • Ding, F.1    Dokholyan, N.V.2    Buldyrev, S.V.3    Stanley, H.E.4    Shakhnovich, E.I.5
  • 13
    • 0035823119 scopus 로고    scopus 로고
    • Understanding hierarchical protein evolution from first principles
    • N.V. Dokholyan, and E.I. Shakhnovich Understanding hierarchical protein evolution from first principles J. Mol. Biol. 312 2001 289 307
    • (2001) J. Mol. Biol. , vol.312 , pp. 289-307
    • Dokholyan, N.V.1    Shakhnovich, E.I.2
  • 14
    • 0032443390 scopus 로고    scopus 로고
    • Discrete molecular dynamics studies of the folding of a protein-like model
    • N.V. Dokholyan, S.V. Buldyrev, H.E. Stanley, and E.I. Shakhnovich Discrete molecular dynamics studies of the folding of a protein-like model Fold. Des. 3 1998 577 587
    • (1998) Fold. Des. , vol.3 , pp. 577-587
    • Dokholyan, N.V.1    Buldyrev, S.V.2    Stanley, H.E.3    Shakhnovich, E.I.4
  • 17
    • 4344704080 scopus 로고    scopus 로고
    • Reassessing random-coil statistics in unfolded proteins
    • N.C. Fitzkee, and G.D. Rose Reassessing random-coil statistics in unfolded proteins Proc. Natl. Acad. Sci. USA 101 2004 12497 12502
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 12497-12502
    • Fitzkee, N.C.1    Rose, G.D.2
  • 18
    • 1342268081 scopus 로고    scopus 로고
    • Steric restrictions in protein folding: An alpha-helix cannot be followed by a contiguous beta-strand
    • N.C. Fitzkee, and G.D. Rose Steric restrictions in protein folding: an alpha-helix cannot be followed by a contiguous beta-strand Protein Sci. 13 2004 633 639
    • (2004) Protein Sci. , vol.13 , pp. 633-639
    • Fitzkee, N.C.1    Rose, G.D.2
  • 20
    • 0020972782 scopus 로고
    • Theoretical studies of protein folding
    • N. Go Theoretical studies of protein folding Annu. Rev. Biophys. Bioeng. 12 1983 183 210
    • (1983) Annu. Rev. Biophys. Bioeng. , vol.12 , pp. 183-210
    • Go, N.1
  • 21
    • 0037424614 scopus 로고    scopus 로고
    • Computational simulation of the statistical properties of unfolded proteins
    • D.P. Goldenberg Computational simulation of the statistical properties of unfolded proteins J. Mol. Biol. 326 2003 1615 1633
    • (2003) J. Mol. Biol. , vol.326 , pp. 1615-1633
    • Goldenberg, D.P.1
  • 23
    • 4243127473 scopus 로고
    • Critical exponents for the n-vector model in three dimensions from field theory
    • J.C. Le Guillou, and J. Zinn-Justin Critical exponents for the n-vector model in three dimensions from field theory Phys. Rev. Lett. 39 1977 95 98
    • (1977) Phys. Rev. Lett. , vol.39 , pp. 95-98
    • Le Guillou, J.C.1    Zinn-Justin, J.2
  • 24
    • 0002006297 scopus 로고
    • Are there pathways for protein folding?
    • C. Levinthal Are there pathways for protein folding? J. Chem. Phys. 65 1968 44 45
    • (1968) J. Chem. Phys. , vol.65 , pp. 44-45
    • Levinthal, C.1
  • 25
    • 0033730431 scopus 로고    scopus 로고
    • The Flory isolated-pair hypothesis is not valid for polypeptide chains: Implications for protein folding
    • R.V. Pappu, R. Srinivasan, and G.D. Rose The Flory isolated-pair hypothesis is not valid for polypeptide chains: implications for protein folding Proc. Natl. Acad. Sci. USA 97 2000 12565 12570
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 12565-12570
    • Pappu, R.V.1    Srinivasan, R.2    Rose, G.D.3
  • 26
    • 0035919635 scopus 로고    scopus 로고
    • Persistence of native-like topology in a denatured protein in 8 M urea
    • D. Shortle, and M.S. Ackerman Persistence of native-like topology in a denatured protein in 8 M urea Science 293 2001 487 489
    • (2001) Science , vol.293 , pp. 487-489
    • Shortle, D.1    Ackerman, M.S.2
  • 27
    • 0037058965 scopus 로고    scopus 로고
    • Methinks it is like a folding curve
    • R. Srinivasan, and G.D. Rose Methinks it is like a folding curve Biophys. Chem. 101-102 2002 167 171
    • (2002) Biophys. Chem. , vol.101-102 , pp. 167-171
    • Srinivasan, R.1    Rose, G.D.2
  • 29
    • 0033554852 scopus 로고    scopus 로고
    • Hydrodynamic radii of native and denatured proteins measured by pulse field gradient NMR techniques
    • D.K. Wilkins, S.B. Grimshaw, V. Receveur, C.M. Dobson, J.A. Jones, and L.J. Smith Hydrodynamic radii of native and denatured proteins measured by pulse field gradient NMR techniques Biochemistry 38 1999 16424 16431
    • (1999) Biochemistry , vol.38 , pp. 16424-16431
    • Wilkins, D.K.1    Grimshaw, S.B.2    Receveur, V.3    Dobson, C.M.4    Jones, J.A.5    Smith, L.J.6
  • 31
    • 0034705338 scopus 로고    scopus 로고
    • NMR characterization of residual structure in the denatured state of protein L
    • Q. Yi, M.L. Scalley-Kim, E.J. Alm, and D. Baker NMR characterization of residual structure in the denatured state of protein L J. Mol. Biol. 299 2000 1341 1351
    • (2000) J. Mol. Biol. , vol.299 , pp. 1341-1351
    • Yi, Q.1    Scalley-Kim, M.L.2    Alm, E.J.3    Baker, D.4
  • 32
    • 0031475159 scopus 로고    scopus 로고
    • Folding thermodynamics of a model three-helix-bundle protein
    • Y.Q. Zhou, and M. Karplus Folding thermodynamics of a model three-helix-bundle protein Proc. Natl. Acad. Sci. USA 94 1997 14429 14432
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 14429-14432
    • Zhou, Y.Q.1    Karplus, M.2
  • 33
    • 0033527768 scopus 로고    scopus 로고
    • Folding of a model three-helix bundle protein: A thermodynamic and kinetic analysis
    • Y.Q. Zhou, and M. Karplus Folding of a model three-helix bundle protein: a thermodynamic and kinetic analysis J. Mol. Biol. 293 1999 917 951
    • (1999) J. Mol. Biol. , vol.293 , pp. 917-951
    • Zhou, Y.Q.1    Karplus, M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.