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Volumn 276, Issue 2, 2000, Pages 393-398

Is the unfolded state the Rosetta Stone of the protein folding problem?

Author keywords

Hydrophobic interactions; Random coil; Residual structure; Secondary structure preference

Indexed keywords

ALPHA HELIX; HYDROPHOBICITY; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN SECONDARY STRUCTURE; REVIEW;

EID: 0034710835     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1006/bbrc.2000.3360     Document Type: Review
Times cited : (35)

References (40)
  • 9
    • 0028856228 scopus 로고
    • The equilibrium folding pathway of staphylococcal nuclease: Identification of the most stable chain-chain interactions by NMR and CD spectroscopy
    • (1995) Biochemistry , vol.34 , pp. 15895-15905
    • Wang, Y.1    Shortle, D.2
  • 12
    • 0030628174 scopus 로고    scopus 로고
    • Residual helical and turn structure in the denatured state of staphylococcal nuclease: Analysis of peptide fragments
    • (1997) Folding Design , vol.2 , pp. 93-100
    • Wang, Y.1    Shortle, D.2
  • 14
  • 18
    • 0027772180 scopus 로고
    • Urea-induced unfolding of the alpha subunit of tryptophan synthase: One-dimensional proton NMR evidence for residual structure near histidine-92 at high denaturant concentration
    • (1993) Biochemistry , vol.32 , pp. 13981-13990
    • Saab-Rincon, G.1    Froebe, C.L.2    Matthews, C.R.3
  • 24
    • 0032939806 scopus 로고    scopus 로고
    • WW: An isolated three-stranded antiparallel beta-sheet domain that unfolds and refolds reversibly: Evidence for a structured hydrophobic cluster in urea and GdnHCl and a disordered thermal unfolded state
    • (1999) Protein Sci. , vol.8 , pp. 841-853
    • Koepf, E.K.1    Petrassi, H.M.2    Sudol, M.3    Kelly, J.W.4
  • 37
    • 0029786948 scopus 로고    scopus 로고
    • A dynamic bundle of four adjacent hydrophobic segments in the denatured state of staphylococcal nuclease
    • (1996) Protein Sci. , vol.5 , pp. 1898-1906
    • Wang, Y.1    Shortle, D.2
  • 38
    • 0031585992 scopus 로고    scopus 로고
    • Characterization of long-range structure in the denatured state of staphylococcal nuclease. II. Distance restraints from paramagnetic relaxation and calculation of an ensemble of structures
    • (1997) J. Mol. Biol. , vol.268 , pp. 170-184
    • Gillespie, J.R.1    Shortle, D.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.