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Volumn 19, Issue 1, 2001, Pages 94-101

Experimental approaches to protein folding based on the concept of a slow hydrogen exchange core

Author keywords

[No Author keywords available]

Indexed keywords

CONFORMATIONS; HYDROGEN; MUTAGENS; PERTURBATION TECHNIQUES; PROTEINS;

EID: 0035015535     PISSN: 10933263     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1093-3263(00)00131-5     Document Type: Article
Times cited : (6)

References (33)
  • 13
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    • NMR Characterization of partially folded and unfolded conformational ensembles of proteins
    • (1999) Biopolymers , vol.51 , pp. 191-207
    • Barbar, E.1
  • 16
    • 0028856228 scopus 로고
    • The equilibrium folding pathway of staphlococcal 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
  • 19
    • 0024414134 scopus 로고
    • The concentration dependence of the diffusion coefficient for BPTI: A dynamic light scattering study of a small protein
    • (1989) Biopolymers , vol.28 , pp. 2001-2024
    • Gallagher, W.1    Woodward, C.2
  • 31
    • 0027136215 scopus 로고
    • Local conformations of peptides representing the entire sequence of bovine pancreatic trypsin inhibitor and their roles in folding
    • (1993) J. Mol. Biol. , vol.234 , pp. 861-878
    • Kemmink, J.1    Creighton, T.E.2
  • 33
    • 0003166498 scopus 로고    scopus 로고
    • Protein folding in the landscape perspective: Chevron plots and non-Arrhenius kinetics
    • (1998) Proteins , vol.30 , pp. 2-33
    • Chan, H.S.1    Dill, K.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.