TY  - JOUR
ID  - open513
UR  - http://onlinelibrary.wiley.com/doi/10.1002/bip.21511/pdf
IS  - 11
A1  - Kumar, Nigam
A1  - Venugopalan, P
A1  - Kishore, Raghuvansh
N2  - 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 ?-aminobutyric acid: Boc-Pro-?-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.
VL  - 93
TI  - Crystallographically observed folded topology of an unsubstituted ?-aminobutyric acid incorporated in a model peptide: importance of a C--H···O interaction.
AV  - restricted
EP  - 31
N1  - Copyright of this article belongs to Wiley
Y1  - 2010/11//
PB  - Wiley
JF  - Biopolymers
KW  - unsubstituted g-aminobutyric acid; unusual
folded conformation; X-ray diffraction; FT-IR;
hydrogen bonded structure
SN  - 0006-3525
SP  - 927
ER  -