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Proline‐containing β‐turns in peptides and...
Journal article

Proline‐containing β‐turns in peptides and proteins. II. Physicochemical studies on tripeptides with the Pro‐Gly sequence

Abstract

Abstract Amino acids are known to differ in their individual preferences for each of the four positions of the β‐turn conformation formed by tetrapeptide segments. Proline and glycine show relatively high preferences for positions 2 and 3, respectively, of the β‐turn. Using tripeptides of the type N ‐acetyl‐Pro‐Gly‐ X ‐OH, where X = Gly, Ala, Leu, Ile, and Phe, we have sought to study the influence of the 4th residue X on the stability of the …

Authors

Brahmachari SK; Rapaka RS; Bhatnagar RS; Ananthanarayanan VS

Journal

Biopolymers, Vol. 21, No. 6, pp. 1107–1125

Publisher

Wiley

Publication Date

June 1982

DOI

10.1002/bip.360210608

ISSN

0006-3525