Issue 11, 1990

Linear oligopeptides. Part 227. X-Ray crystal and molecular structures of two α-helix-forming (Aib-L-Ala)sequential oligopeptides, pBrBz-(Aib-L-Ala)5-OMe and pBrBz-(Aib-L-Ala)6-OMe

Abstract

A crystal-state structutal analysis of pBrBz-(Aib-LAla)5-OMe tetrahydrate and pBrBz-(Aib-L-Ala)6-OMe dihydrate has been performed by X-ray diffraction. The decapeptide and dodecapeptide molecules are both basically α-helical with five and seven 1 â†� 5 intramolecular H-bonds, respectively. A similarity between the two structures is also seen near the C-terminus, where regularity of the α-helix is disrupted in favour of formation of intramolecular H-bonds of the 1 â†� 4 and 1 â†� 6 types. A brief comparison with parameters and interactions characteristic of the helices present in globular proteins has been made.

Article information

Article type
Paper

J. Chem. Soc., Perkin Trans. 2, 1990, 1829-1837

Linear oligopeptides. Part 227. X-Ray crystal and molecular structures of two α-helix-forming (Aib-L-Ala)sequential oligopeptides, pBrBz-(Aib-L-Ala)5-OMe and pBrBz-(Aib-L-Ala)6-OMe

E. Benedetti, B. Di Blasio, V. Pavone, C. Pedone, A. Santini, A. Bavoso, C. Toniolo, M. Crisma and L. Sartore, J. Chem. Soc., Perkin Trans. 2, 1990, 1829 DOI: 10.1039/P29900001829

To request permission to reproduce material from this article, please go to the Copyright Clearance Center request page.

If you are an author contributing to an RSC publication, you do not need to request permission provided correct acknowledgement is given.

If you are the author of this article, you do not need to request permission to reproduce figures and diagrams provided correct acknowledgement is given. If you want to reproduce the whole article in a third-party publication (excluding your thesis/dissertation for which permission is not required) please go to the Copyright Clearance Center request page.

Read more about how to correctly acknowledge RSC content.

Spotlight

Advertisements