TY  - JOUR
ID  - open366
UR  - http://www.sciencedirect.com/science/article/pii/S0014579397012398
IS  - 1
A1  - Ganguly, Ashish
A1  - Kishore, Raghuvansh
N2  - Thermodynamic investigations of a smallest possible intramolecularly hydrogen bonded C5-structure, across a Thr residue, in model peptides Boc-Xxx-Thr-NH2 (Xxx = Ile, 1 or Leu, 2), indicated unusual thermal stability of the structure in non-polar medium. An analysis of van't Hoff plots, constructed from variable temperature 1H NMR data, yielded the thermodynamic parameters of a hydrogen bonded five-membered ring. The non-significance of the spatial organizations of the preceding CdeltaH3 bearing hydrophobic proteinogenic residue on the thermal stability of the C5-structure has been observed. The results revealed that the contribution of this element of secondary structure is quantifiable and the stability appeared to be roughly comparable to other intramolecularly hydrogen bonded reverse turn structures frequently observed in polypeptides and proteins.
VL  - 417
TI  - Thermodynamic characterizations of an intramolecularly hydrogen bonded C5-structure across proteinogenic residue.
AV  - restricted
EP  - 100
N1  - Copyright of this article belongs to Elsevier Science
Y1  - 1997/11/03/
PB  - Elsevier Science/Academic Press
JF  - FEBS letters
KW  - C5-structure; NMR
KW  -  1H- spectroscopy; van't Hoff analysis; ?- and ?-turn secondary structure
SN  - 0014-5793
SP  - 97
ER  -