A 13C spin‐lattice relaxation study of dipeptides containing glycine and proline: Mobility of the cyclic proline side chain

Abstract
Molecular dynamics of the cyclic dipeptides cyclo(Gly‐L‐Pro), cyclo‐(L‐Pro‐L‐Pro), and cyclo(L‐Pro‐D‐Pro) and the linear dipeptides L‐Pro‐Gly and cis and trans Gly‐L‐Pro were studied in neutral aqueous solution by 13C nuclear magnetic resonance. Spinlattice relaxation times (T1) were determined for each individual carbon atom. The correlation times, τ, were derived from a semiquantitative analysis of the T1 data. The correlation times of the proline ring carbons, β, γ, and δ suggest that the cyclic dipeptides have more restriction of conformational freedom in the proline ring than the linear dipeptides. This effect is most pronounced on the γ carbon.

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