Crystallographically observed folded topology of an unsubstituted γ-aminobutyric acid incorporated in a model peptide: importance of a C--H···O interaction.

Kumar, Nigam and Venugopalan, P and Kishore, Raghuvansh (2010) Crystallographically observed folded topology of an unsubstituted γ-aminobutyric acid incorporated in a model peptide: importance of a C--H···O interaction. Biopolymers, 93 (11). pp. 927-31. ISSN 0006-3525

PDF kishore10.pdf - Published Version Restricted to Registered users only Download (244Kb) | Request a copy

Abstract

To validate the existing hypothesis put forward by Navarro et al., we performed single crystal X-ray diffraction structural analysis of a designed model peptide incorporating an unsubstituted achiral γ-aminobutyric acid: Boc-Pro-γ-Abu-OH (1) lacking C-terminal amide group. The analysis established existence of an overall unusual tightly folded topology stabilized by a conventional N(i)···H--N(i + 1) and an unconventional C(i)--H···O(i) type intramolecular hydrogen bonding interactions, encompassing a five-membered and a six-membered ring motifs, respectively. Moreover, in conjunction with Fourier transform infrared (FT-IR) absorption study in solid KBr, the results provided evidence that two conventional and one unconventional noncovalent intermolecular interaction stabilize a right-handed helical architecture generated via molecular self-assembly by translating the symmetry related molecules along the crystallographic b axis. © 2010 Wiley Periodicals, Inc. Biopolymers 93: 927-931, 2010.

Item Type:	Article
Additional Information:	Copyright of this article belongs to Wiley
Uncontrolled Keywords:	unsubstituted g-aminobutyric acid; unusual folded conformation; X-ray diffraction; FT-IR; hydrogen bonded structure
Subjects:	Q Science > QD Chemistry
Depositing User:	Dr. K.P.S.Sengar
Date Deposited:	08 Dec 2011 19:17
Last Modified:	09 Jan 2015 10:43
URI:	http://crdd.osdd.net/open/id/eprint/513

Actions (login required)

View Item