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

DIR@IMTECH: CSIR-Institute of Microbial Technology

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Title Crystallographically observed folded topology of an unsubstituted γ-aminobutyric acid incorporated in a model peptide: importance of a C--H···O interaction.
 
Creator Kumar, Nigam
Venugopalan, P
Kishore, Raghuvansh
 
Subject QD Chemistry
 
Description 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.
 
Publisher Wiley
 
Date 2010-11
 
Type Article
PeerReviewed
 
Format application/pdf
 
Identifier http://crdd.osdd.net/open/513/1/kishore10.pdf
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
 
Relation http://onlinelibrary.wiley.com/doi/10.1002/bip.21511/pdf
http://crdd.osdd.net/open/513/