Brahmachari, Samir K and Rapaka, Rao S and Bhatnagar, Rajendra S and Ananthanarayanan, VS (1982) Proline-containing \beta-turns in peptides and proteins. II. Physicochemical studies on tripeptides with the Pro-Gly sequence. In: Biopolymers, 21 (6). pp. 1107-1125.
Amino acids are known to differ in their individual preferences for each of the four positions of the ?-turn conformation formed by tetrapeptide segments. Proline and glycine show relatively high preferences for positions 2 and 3, respectively, of the \beta -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 \beta -turn conformation in these tripeptides. Our nmr and CD results show that the \beta -turn stability is quite significantly governed by the nature of the amino acid residue at this position in the following order: Leu > Ala > Ile, Gly > Phe.
|Item Type:||Journal Article|
|Additional Information:||The copyright belongs to John Wiley & Sons, Inc.|
|Department/Centre:||Division of Biological Sciences > Molecular Biophysics Unit|
|Date Deposited:||08 Dec 2005|
|Last Modified:||19 Sep 2010 04:21|
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