Conformational analysis of small disulfide loops. Spectroscopic and theoretical studies on a synthetic cyclic tetrapeptide containing cystine
Data(s) |
1982
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Resumo |
The conformational analysis of the synthetic peptide Boc-Cys-Pro-Val-Cys-NHMe has been carried out, as a model for small disulfide loops, in biologically active polypeptides. 'H NMR studies (270 MHz) establish that the Val(3) and Cys(4) NH groups are solvent shielded, while 13C studies establish an all-trans peptide backbone. Circular dichroism and Raman spectroscopy provide evidence for a right-handed twist of the disulfide bond. Analysis of the vicinal (JaB)c oupling constants for the two Cys residues establishes that XI - *60° for Cys(4), while some flexibility is suggested at Cys( 1). Conformational energy calculations, imposing intramolecular hydrogen bonding constraints, favor a P-turn (type I) structure with Pro(2)-Va1(3) as the corner residues. Theoretical and spectroscopic results are consistent with the presence of a transannular 4 - 1 hydrogen bond between Cys( 1) CO and Cys(4) NH groups, with the Val NH being sterically shielded from the solvent environment. |
Formato |
application/pdf |
Identificador |
http://eprints.iisc.ernet.in/20449/1/fulltext.pdf Venkatachalapath, YV and Prasad, B V Venkataram and Balaram, P (1982) Conformational analysis of small disulfide loops. Spectroscopic and theoretical studies on a synthetic cyclic tetrapeptide containing cystine. In: Biochemistry, 21 (22). pp. 5502-5509. |
Publicador |
American Chemical Society |
Relação |
http://pubs.acs.org/doi/pdf/10.1021/bi00265a019 http://eprints.iisc.ernet.in/20449/ |
Palavras-Chave | #Molecular Biophysics Unit |
Tipo |
Journal Article PeerReviewed |