FOLDING OF AMINOSUCCINYL PEPTIDES - THERMODYNAMIC DATA FROM TEMPERATURE-DEPENDENT CIRCULAR-DICHROISM MEASUREMENTS

Citation
S. Capasso et al., FOLDING OF AMINOSUCCINYL PEPTIDES - THERMODYNAMIC DATA FROM TEMPERATURE-DEPENDENT CIRCULAR-DICHROISM MEASUREMENTS, Chirality, 7(8), 1995, pp. 605-609
Citations number
35
Language
INGLESE
art.tipo
Article
Categorie Soggetti
Pharmacology & Pharmacy",Chemistry
Journal title
Chirality → ACNP
ISSN journal
0899-0042
Volume
7
Issue
8
Year of publication
1995
Pages
605 - 609
Database
ISI
SICI code
0899-0042(1995)7:8<605:FOAP-T>2.0.ZU;2-I
Abstract
The conformational equilibrium of aminosuccinyl peptides between exten ded conformations acid an intramolecularly hydrogen bonded type II' be ta-turn conformation has been studied on the peptide Boc-L-Asu-Gly-L-A la-OMe (Asu = aminosuccinyl residue) by means of temperature dependenc e of circular dichroism spectra.Owing to the peculiar chiroptical and conformational properties of the Asu residue, this technique proved to be very useful for deriving thermodynamic data for the above folding process, The value of Delta H-o (-6.6 kJ mol(-1)), obtained for the pe ptide studied in a chloroform-acetonitrile mixture, shows that the low er energy of the folded conformer is primarily due to the characterist ic intramolecular hydrogen bond of the beta turns. (C) 1995 Wiley-Liss , Inc.