Conformations of cyclic octapeptides. 4. Diastereomers of cyclo(Gly-Pro-Phe-Ala-Asn-Ala-Val-Ser).
Stereoisomers of cyclo(Gly-Pro-Phe-Ala-Asn-Ala-Val-Ser) were synthesized. NMR studies of their solution conformations, focusing on peptide N-H solvent exposure, were made. These indicated that a single proline residue in the cyclic octapeptide ring is insufficient constraint to stabilize the backbone conformations that were previously established for cyclo(Gly-Pro-Phe-Ala)2.
D007202:Indicators and Reagents; D009682:Magnetic Resonance Spectroscopy; D008958:Models, Molecular; D010456:Peptides, Cyclic / Q000138:chemical synthesis*; D011487:Protein Conformation; D013237:Stereoisomerism
D007202:Indicators and Reagents; D010456:Peptides, Cyclic; C051115:cyclo(glycyl-prolyl-phenylalanyl-alanyl-asparaginyl-alanyl-valyl-seryl)