Conformations Of Peptides Containing 1-Aminocyclohexane-Carboxylic Acid (Acc6) - Crystal-Structures Of 2 Model Peptides

Bardi, R and Piazzesi, AM and Toniolo, C and Sukumar, M and Raj, PA and Balaram, P (1985) Conformations Of Peptides Containing 1-Aminocyclohexane-Carboxylic Acid (Acc6) - Crystal-Structures Of 2 Model Peptides. In: International Journal Of Peptide And Protein Research, 25 (6). pp. 628-639.

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Abstract

The crystal structures of two peptides containing 1-aminocyclohexanecarboxylic acid (Acc6) are described. Boc-Aib-Acc6-NHMe · H2O adopts a β-turn conformation in the solid state, stabilized by an intramolecular 4 → 1 hydrogen bond between the Boc CO and methylamide NH groups. The backbone conformational angles (φAib = – 50.3°, ψAib = – 45.8°; φAcc6 = – 68.4°, ψAcc6 = – 15°) lie in between the values expected for ideal Type I or III β-turns. In Boc-Aib-Acc6-OMe, the Aib residue adopts a partially extended conformation (φAib = – 62.2°, ψAib = 143°) while the Acc6residue maintains a helical conformation (φAcc6 = 48°, ψAcc6= 42.6°). 1H n.m.r. studies in CDCl3 and (CD3)2SO suggest that Boc-Aib-Acc6-NHMe maintains the β-turn conformation in solution.

Item Type:	Journal Article
Publication:	International Journal Of Peptide And Protein Research
Publisher:	Munksgaard Int Publ Ltd
Additional Information:	The copyright of this article belongs to Munksgaard Int Publ Ltd.
Department/Centre:	Division of Biological Sciences > Molecular Biophysics Unit
Date Deposited:	02 Jul 2009 13:23
Last Modified:	19 Sep 2010 05:35
URI:	http://eprints.iisc.ac.in/id/eprint/20936

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