N.m.r. studies of internal mobility in a cyclic tetrapeptide

Abstract
The conformation of cyclo(D‐Phe‐D‐Pro‐Ala‐Pro) is reported. Measurements of spin‐lattice relaxation in the rotating frame indicate that this peptide is conformationally less mobile on the microsecond time scale than larger cyclic peptides previously studied. Libration of the Pro‐Ala and Pro‐Phe peptide bond planes is suggested as the source of the small exchange contributions to 1/T.

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