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
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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 |
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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 |
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