TY  - JOUR
ID  - open311
UR  - http://onlinelibrary.wiley.com/doi/10.1034/j.1399-3011.2000.00737.x/abstract
IS  - 1
A1  - Thakur, A K
A1  - Venugopalan, P
A1  - Kishore, Raghuvansh
N2  - Crystal structure analysis of a model peptide: Boc-beta-Ala-Aib-beta-Ala-NHCH3 (beta-Ala: 3-amino propionic acid; Aib: alpha-aminoisobutyric acid) revealed distinct conformational preferences for folded [phi approximately 136 degrees, mu approximately -62 degrees, psi approximately 100 degrees] and semifolded [phi approximately 83 degrees, mu approximately -177 degrees, psi approximately -117 degrees] structures of the N-and C-terminus beta-Ala residues, respectively. The overall folded conformation is stabilized by unusual Ni...H-Ni+1 and nonconventional C-H...O intramolecular hydrogen bonding interactions.
VL  - 56
TI  - Entrapping unusual folding characteristics of the beta-Ala residues in a model peptide: Boc-beta-Ala-Aib-beta-Ala-NHCH3.
AV  - restricted
EP  - 8
N1  - Copyright of this article belongs to Wiley.
Y1  - 2000/07//
PB  - Wiley
JF  - The journal of peptide research : official journal of the American Peptide Society
KW  - b-Ala peptides; folded structures; peptide design;
unusual H-bond; X-ray diffraction analysis
SN  - 1397-002X
SP  - 55
ER  -