TY  - JOUR
N1  - Copyright of this article belongs to Elsevier Science.
ID  - open863
UR  - http://dx.doi.org/10.1016/S0040-4039(01)00788-2
IS  - 28
A1  - Thakur, A K
A1  - Kishore, Raghuvansh
Y1  - 2001///
N2  - X-Ray diffraction analysis of the model peptide Boc-Thr-Thr-OCH3 reveals the existence of distinctive conformational characteristics: semi-extended (?=?62.1°; ?=137.1°) and semi-folded (?=?130.3°; ?T=5.7°) of the N- and C-terminus Thr residues, respectively. Surprisingly, an overall significantly ?flat? conformation is stabilised by a number of novel main-chain to side-chain intramolecular hydrogen bonds, i.e. two non-conventional: C?i+1?H?O?Ci?1 and C?i?H?Oi+1 types and two conventional: Ni?H?O?i and O?i?H?Ni types of interactions
PB  - Elsevier Science
JF  - Tetrahedron Letters
VL  - 42
SN  - 00404039
TI  - Crystallographic characterisation of novel ?-turn like folds in a model peptide: stabilisation by main-chain to side-chain interactions
SP  - 4691
AV  - restricted
EP  - 4694
ER  -