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Abstract
A slow conformational equilibrium, commensurable with the retention times, was shown to induce peak broadening or peak splitting during reversed-phase high-performance liquid chromatography of several medium-sized peptides. Elution at 50°C resulted in sharp unique peaks, while at sub-ambient temperature well resolved peaks were observed. Linear peptides which show this phenomenon had a Pro-Pro bond, but the phenomenon was also observed in the case of a cyclic peptide containing two non-vicinal proline residues.
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