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Comparison of conformational properties of proline and threonine residues.

作者信息

Siemion I Z, Sobczyk K, Lisowski M

出版信息

Int J Pept Protein Res. 1986 Feb;27(2):127-37. doi: 10.1111/j.1399-3011.1986.tb01802.x.

DOI:10.1111/j.1399-3011.1986.tb01802.x
PMID:3084397
Abstract

The conformational role of Thr was investigated by 13C-n.m.r. and CD methods using a following series of tetrapeptides: Thr-Ala-Ala-Ala, Ala-Thr-Ala-Ala, Ala-Ala-Thr-Ala and Ala-Ala-Ala-Thr. It was found that introduction of Thr in every position of the tetraalanine peptide chain distinctly influences conformational equilibria of the peptides. An increase of beta-turn forms in conformational equilibria is induced by ionization of the terminal carboxyl group, independent of threonine position in the peptide chain. Threonine in position 1 or 3 of the peptide chain seems to have some importance for beta-turn formation in acid solution.

摘要

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