메뉴 건너뛰기




Volumn 430, Issue 6999, 2004, Pages 586-590

Low-populated folding intermediates of Fyn SH3 characterized by relaxation dispersion NMR

Author keywords

[No Author keywords available]

Indexed keywords

BIOCHEMICAL ENGINEERING; DISPERSIONS; ENZYMES; MUTAGENESIS; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PROTEINS; REACTION KINETICS;

EID: 3242880292     PISSN: 00280836     EISSN: None     Source Type: Journal    
DOI: 10.1038/nature02655     Document Type: Article
Times cited : (420)

References (28)
  • 3
    • 0037418635 scopus 로고    scopus 로고
    • Hammond behavior versus ground state effects in protein folding: Evidence for narrow free energy barriers and residual structure in unfolded states
    • Sanchez, I. E. & Keifhaber, T. Hammond behavior versus ground state effects in protein folding: Evidence for narrow free energy barriers and residual structure in unfolded states. J. Mol. Biol. 327, 867-884 (2003).
    • (2003) J. Mol. Biol. , vol.327 , pp. 867-884
    • Sanchez, I.E.1    Keifhaber, T.2
  • 4
    • 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 295, 1719-1722 (2002).
    • (2002) Science , vol.295 , pp. 1719-1722
    • Klein-Seetharaman, J.1
  • 5
    • 0026484261 scopus 로고
    • SH2 and SH3 domains: From structure to function
    • Pawson, T. & Gish, G. D. SH2 and SH3 domains: from structure to function. Cell 71, 359-362 (1992).
    • (1992) Cell , vol.71 , pp. 359-362
    • Pawson, T.1    Gish, G.D.2
  • 6
    • 0031815749 scopus 로고    scopus 로고
    • How do small, single domain proteins fold?
    • Jackson, S. E. How do small, single domain proteins fold? Fold. Design 3, R81-R91 (1998).
    • (1998) Fold. Design , vol.3
    • Jackson, S.E.1
  • 7
    • 0347357617 scopus 로고    scopus 로고
    • Protein folding and misfolding
    • Dobson, C. M. Protein folding and misfolding. Nature 426, 884-890 (2003).
    • (2003) Nature , vol.426 , pp. 884-890
    • Dobson, C.M.1
  • 8
    • 0037686252 scopus 로고    scopus 로고
    • The present view of the mechanism of protein folding
    • Daggett, V. & Fersht, A. R. The present view of the mechanism of protein folding. Nature Rev. Mol. Cell Biol. 4, 497-502 (2003).
    • (2003) Nature Rev. Mol. Cell Biol. , vol.4 , pp. 497-502
    • Daggett, V.1    Fersht, A.R.2
  • 9
    • 0036172116 scopus 로고    scopus 로고
    • Hydrophobic core packing in the SH3 domain folding transition state
    • Northey, J. G. B., Di Nardo, A. A. & Davidson, A. R. Hydrophobic core packing in the SH3 domain folding transition state. Nature Struct. Biol. 9, 126-130 (2002).
    • (2002) Nature Struct. Biol. , vol.9 , pp. 126-130
    • Northey, J.G.B.1    Di Nardo, A.A.2    Davidson, A.R.3
  • 10
    • 0032562182 scopus 로고    scopus 로고
    • The folding kinetics and thermodynamics of the Fyn-SH3 domain
    • Plaxo, K. W. et al. The folding kinetics and thermodynamics of the Fyn-SH3 domain. Biochemistry 37, 2529-2537 (1998).
    • (1998) Biochemistry , vol.37 , pp. 2529-2537
    • Plaxo, K.W.1
  • 11
    • 0032750509 scopus 로고    scopus 로고
    • The folding transition state between SH3 domains is conformationally restricted and evolutionarily conserved
    • Martinez, J. C. & Serrano, L. The folding transition state between SH3 domains is conformationally restricted and evolutionarily conserved. Nature Struct. Biol. 6, 1010-1016 (1999).
    • (1999) Nature Struct. Biol. , vol.6 , pp. 1010-1016
    • Martinez, J.C.1    Serrano, L.2
  • 14
    • 0034919305 scopus 로고    scopus 로고
    • NMR methods for quantifying microsecond-to-millisecond motions in biological macromolecules
    • Palmer, A. G., Kroenke, C. D. & Loria, J. P. NMR methods for quantifying microsecond-to-millisecond motions in biological macromolecules. Methods Enzymol. 339, 204-238 (2001).
    • (2001) Methods Enzymol. , vol.339 , pp. 204-238
    • Palmer, A.G.1    Kroenke, C.D.2    Loria, J.P.3
  • 16
    • 0029395478 scopus 로고
    • Win some, lose some. Enthalpy-entropy compensation in weak intermolecular interactions
    • Dunitz, J. D. Win some, lose some. Enthalpy-entropy compensation in weak intermolecular interactions. Chem. Biol. 2, 709-712 (1995).
    • (1995) Chem. Biol. , vol.2 , pp. 709-712
    • Dunitz, J.D.1
  • 17
    • 0028981210 scopus 로고
    • Negative activation enthalpies on the kinetics of protein folding
    • Oliveberg, M., Tan, Y. J. & Fersht, A. R. Negative activation enthalpies on the kinetics of protein folding. Proc Natl Acad. Sci. USA 92, 8926-8929 (1995).
    • (1995) Proc Natl Acad. Sci. USA , vol.92 , pp. 8926-8929
    • Oliveberg, M.1    Tan, Y.J.2    Fersht, A.R.3
  • 18
    • 0344301982 scopus 로고    scopus 로고
    • Protein folding: A perspective from theory and experiment
    • Dobson, C. M., Sali, A. & Karplus, M. Protein folding: A perspective from theory and experiment. Angew. Chem. Int. Edn Engl. 37, 867-893 (1998).
    • (1998) Angew. Chem. Int. Edn Engl. , vol.37 , pp. 867-893
    • Dobson, C.M.1    Sali, A.2    Karplus, M.3
  • 19
    • 0035252350 scopus 로고    scopus 로고
    • Three key residues from a critical contact network in a protein folding transition state
    • Vendruscolo, M., Paci, E., Dobson, C. M. & Karplus, M. Three key residues from a critical contact network in a protein folding transition state. Nature 409, 641-645 (2001).
    • (2001) Nature , vol.409 , pp. 641-645
    • Vendruscolo, M.1    Paci, E.2    Dobson, C.M.3    Karplus, M.4
  • 20
    • 0037114648 scopus 로고    scopus 로고
    • 13C′ chemical shifts in peptides using density functional theory
    • 13C′ chemical shifts in peptides using density functional theory. Biopolymers 65, 408-423 (2002).
    • (2002) Biopolymers , vol.65 , pp. 408-423
    • Xu, X.P.1    Case, D.A.2
  • 21
    • 0036296248 scopus 로고    scopus 로고
    • Probing folding kinetics beyond the Phi value: Using multiple amino acid substitutions to investigate the structure of the SH 3 domain folding transition state
    • Northey, J. G. B., Maxwell, K. L. & Davidson, A. R. Probing folding kinetics beyond the Phi value: Using multiple amino acid substitutions to investigate the structure of the SH3 domain folding transition state. J. Mol. Biol. 320, 389-402 (2002).
    • (2002) J. Mol. Biol. , vol.320 , pp. 389-402
    • Northey, J.G.B.1    Maxwell, K.L.2    Davidson, A.R.3
  • 22
    • 0032542018 scopus 로고    scopus 로고
    • Mutagenesis of a buried polar interaction in an SH3 domain: Sequence conservation provides the best prediction of stability effects
    • Maxwell, K. L. & Davidson, A. R. Mutagenesis of a buried polar interaction in an SH3 domain: sequence conservation provides the best prediction of stability effects. Biochemistry 37, 16172-16182 (1998).
    • (1998) Biochemistry , vol.37 , pp. 16172-16182
    • Maxwell, K.L.1    Davidson, A.R.2
  • 23
    • 0028019827 scopus 로고
    • Multidimensional nuclear magnetic resonance methods for protein studies
    • Bax, A. Multidimensional nuclear magnetic resonance methods for protein studies. Curr. Opin. Struct. Biol. 4, 738-744 (1994).
    • (1994) Curr. Opin. Struct. Biol. , vol.4 , pp. 738-744
    • Bax, A.1
  • 26
    • 0036435907 scopus 로고    scopus 로고
    • Determination of a transition state at atomic resolution from protein engineering data
    • Paci, E., Vendruscolo, M., Dobson, C. M. & Karplus, M. Determination of a transition state at atomic resolution from protein engineering data. J. Mol. Biol. 324, 151-163 (2002).
    • (2002) J. Mol. Biol. , vol.324 , pp. 151-163
    • Paci, E.1    Vendruscolo, M.2    Dobson, C.M.3    Karplus, M.4
  • 27
    • 0027245080 scopus 로고
    • Crystal structure of the SH3 domain in human Fyn; comparison of the three-dimensional structures of SH3 domains in tyrosine kinases and spectrin
    • Noble, M. E., Musacchio, A., Saraste, M., Courtneidge, S. A. & Wierenga, R. K. Crystal structure of the SH3 domain in human Fyn; comparison of the three-dimensional structures of SH3 domains in tyrosine kinases and spectrin. EMBO J. 12, 2617-2624 (1993).
    • (1993) EMBO J. , vol.12 , pp. 2617-2624
    • Noble, M.E.1    Musacchio, A.2    Saraste, M.3    Courtneidge, S.A.4    Wierenga, R.K.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.