Peptide design: influence of a guest Aib-Pro segment on the stereochemistry of an Oligo-Val sequence - solution conformations and crystal structure of Boc-(Val)2-Aib-Pro-(Val)3-OMe

Karle, Isabella L. ; Flippen-Anderson, Judith L. ; Uma, K. ; Balaram, Hemalatha ; Balaram, P. (1990) Peptide design: influence of a guest Aib-Pro segment on the stereochemistry of an Oligo-Val sequence - solution conformations and crystal structure of Boc-(Val)2-Aib-Pro-(Val)3-OMe Biopolymers, 29 (10-11). pp. 1433-1442. ISSN 0006-3525

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Official URL: http://www3.interscience.wiley.com/journal/1075888...

Related URL: http://dx.doi.org/10.1002/bip.360291010

Abstract

The peptide Boc-Val-Val-Aib-Pro-Val-Val-Val-OMe has been synthesized to investigate the effect of introduction of a strong β-turn promoting guest segment into an oligopeptide with a tendency to form extended structures. 1H-nmr studies in solution using analysis of NH group solvent accessibility and nuclear Overhauser effects suggest an appreciable solvent dependence of conformations. In chloroform a 310-helical structure is favored while in dimethylsulfoxide an Aib-Pro -turn with extended arms on either side is suggested. In the crystal, the backbone forms a somewhat distorted 310-helix despite the presence of a Pro residue in the middle. Among the four possible intrahelical hydrogen bonds three are of the 4 →1 type and one 5→ 1. Head-to-tail NH...O=C hydrogen bonds link the helical molecules into continuous columns. The space group is P212121 with a = 11.320(2), b = 19.889(3), and c = 21.247(3) Å.

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