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Volumn 1036, Issue , 2013, Pages 298-304

Spatial structure of cyclosporin A and insight into its flexibility

Author keywords

Chemical exchange; Conformation; Model membranes; Nuclear magnetic resonance; Peptide

Indexed keywords

APOLAR SOLVENTS; CHEMICAL EXCHANGE; CYCLOSPORIN; CYCLOSPORIN A; H NMR SPECTRA; INTRA-MOLECULAR HYDROGEN BONDS; MICELLAR SOLUTION; MODEL MEMBRANES; MOLECULAR DYNAMICS SIMULATIONS; NUCLEAR OVERHAUSER EFFECTS; PEPTIDE BONDS; RESIDUAL DIPOLAR COUPLINGS; SIMULATED RESULTS; SODIUM DODECYL SULPHATE; SPATIAL STRUCTURE; STRUCTURAL DATA; THERMODYNAMIC PARAMETER; TWO-STATE;

EID: 84871574834     PISSN: 00222860     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.molstruc.2012.11.005     Document Type: Article
Times cited : (38)

References (44)
  • 1
    • 84889841716 scopus 로고    scopus 로고
    • Prolyl isomerization in protein folding
    • J. Buchner, T. Kiefhaber, Wiley-VCH Weinheim (Chapter 25)
    • F. Schmid Prolyl isomerization in protein folding J. Buchner, T. Kiefhaber, Protein Folding Handbook 2005 Wiley-VCH Weinheim 916 945 (Chapter 25)
    • (2005) Protein Folding Handbook , pp. 916-945
    • Schmid, F.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.