Comparison of conformational properties of proline and threonine residues
- 1 February 1986
- journal article
- research article
- Published by Wiley in International Journal of Peptide and Protein Research
- Vol. 27 (2) , 127-137
- https://doi.org/10.1111/j.1399-3011.1986.tb01802.x
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.Keywords
This publication has 18 references indexed in Scilit:
- Intrahelical hydrogen bonding of serine, threonine and cysteine residues within α-helices and its relevance to membrane-bound proteinsJournal of Molecular Biology, 1984
- Conformational Investigations in the Tuftsin GroupAnnals of the New York Academy of Sciences, 1983
- Conformation of model, alanine and proline containing tetrapeptides in waterInternational Journal of Peptide and Protein Research, 1983
- Steric effect exerted by the proline residue on the antecedent alanine residueInternational Journal of Peptide and Protein Research, 1982
- β-turns in proteinsJournal of Molecular Biology, 1977
- Molecular orbital calculations on the conformation of polypeptides and proteinsTheoretical Chemistry Accounts, 1970
- Verbesserte Synthese von tert.‐Butyloxycarbonyl‐aminosäuren durch pH‐Stat‐ReaktionEuropean Journal of Organic Chemistry, 1967
- The Use of Esters of N-Hydroxysuccinimide in Peptide SynthesisJournal of the American Chemical Society, 1964
- Amino-acids and peptides. XXXIII. Nitrosyl chloride and butyl nitrite as reagents in peptide synthesis by the azide method; Suppression of amide formationCollection of Czechoslovak Chemical Communications, 1961
- Optical Rotation of Peptides. I. Glycine and Alanine Dipeptides1Journal of the American Chemical Society, 1951