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Volumn 307, Issue 1, 2001, Pages 379-391

Detection of two partially structured species in the folding process of the amyloidogenic protein β2-microglobulin

Author keywords

Amyloid fibrils; Dialysis related amyloidosis; Folding intermediates; Protein folding; 2 microglobulin

Indexed keywords

8 ANILINO 1 NAPHTHALENESULFONIC ACID; AMYLOID; AMYLOID PROTEIN; BETA 2 MICROGLOBULIN; CYCLOPHILIN; GUANIDINE; PROLINE; WATER;

EID: 0035896018     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.2000.4478     Document Type: Article
Times cited : (111)

References (37)
  • 18
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    • Folding of chymotrypsin inhibitor 2. 2. Influence of proline isomerisation on the folding kinetics and thermodynamics characterisation of the transition state of folding
    • (1991) Biochemistry , vol.30 , pp. 10436-10443
    • Jackson, S.E.1    Fersht, A.R.2
  • 31
    • 0023697408 scopus 로고
    • Unfolding free-energy changes determined by the linear extrapolation method. 1. Unfolding of phenyl-methanesulfonyl alpha-chymotrypsin using different denaturants
    • (1988) Biochemistry , vol.27 , pp. 8063-8068
    • Santoro, M.M.1    Bolen, D.W.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.