Abstract:
:The conformational behavior of cyclic peptides of the amino acid sequence Cys-Phe/Ala-Pro-Ala-Cys has been investigated through the combined use of molecular simulation methods and NMR experiments to find models for beta-VIa turns of proteins. Both oxidized (cyclic) peptides and reduced (linear) forms were investigated. At least 95% of the cyclic peptides show a cis conformation of the Xaa-Pro bond in solution in DMSO or water, whereas all other peptide bonds are trans. Furthermore, we observed a hydrogen bond between the NH group of residue Ala4 and the C = O group of residue Cys1. Both properties are indicative of beta-VIa turns. After reduction of the disulfide bridge, the all-trans form of the peptide bonds predominates.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Weisshoff H,Frost K,Brandt W,Henklein P,Mügge C,Frömmel Cdoi
10.1016/0014-5793(95)00982-fsubject
Has Abstractpub_date
1995-09-25 00:00:00pages
203-9issue
2-3eissn
0014-5793issn
1873-3468pii
0014-5793(95)00982-Fjournal_volume
372pub_type
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