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Folding of aminosuccinyl peptides: Thermodynamic data from temperature dependent circular dichroism measurements
Author(s) -
Capasso Sante,
Mazzarella Lelio,
Zagari Adriana
Publication year - 1995
Publication title -
chirality
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.43
H-Index - 77
eISSN - 1520-636X
pISSN - 0899-0042
DOI - 10.1002/chir.530070808
Subject(s) - chemistry , circular dichroism , intramolecular force , conformational isomerism , folding (dsp implementation) , hydrogen bond , vibrational circular dichroism , peptide , crystallography , protein folding , residue (chemistry) , stereochemistry , molecule , organic chemistry , biochemistry , electrical engineering , engineering
Abstract The conformational equilibrium of aminosuccinyl peptides between extended conformations and an intramolecularly hydrogen bonded type II′ β‐turn conformation has been studied on the peptide Boc‐ L ‐Asu‐Gly‐ L ‐Ala‐OMe (Asu = aminosuccinyl residue) by means of temperature dependence 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 Δ H 0 (−6.6 kJ mol −1 ), obtained for the peptide studied in a chloroformacetonitrile mixture, shows that the lower energy of the folded conformer is primarily due to the characteristic intramolecular hydrogen bond of the β turns. © 1995 Wiley‐Liss, Inc.