THERMODYNAMIC PROPERTIES OF PEPTIDE SOLUTIONS .15. PARTIAL MOLAR ISENTROPIC COMPRESSIBILITIES OF SOME GLYCYL DIPEPTIDES IN AQUEOUS-SOLUTIONAT 15 AND 35-DEGREES-C

Citation
Gr. Hedwig et al., THERMODYNAMIC PROPERTIES OF PEPTIDE SOLUTIONS .15. PARTIAL MOLAR ISENTROPIC COMPRESSIBILITIES OF SOME GLYCYL DIPEPTIDES IN AQUEOUS-SOLUTIONAT 15 AND 35-DEGREES-C, Journal of solution chemistry, 25(11), 1996, pp. 1041-1053
Citations number
35
Categorie Soggetti
Chemistry Physical
ISSN journal
00959782
Volume
25
Issue
11
Year of publication
1996
Pages
1041 - 1053
Database
ISI
SICI code
0095-9782(1996)25:11<1041:TPOPS.>2.0.ZU;2-Z
Abstract
The partial molar isentropic compressibilities at infinite dilution, K -s,2(o), have been obtained for eight glycyl dipeptides of sequence gl y-X (X is an amino acid) in aqueous solution at the temperatures 15 an d 35 degrees C. The results have been combined with those obtained at 25 degrees C, that were reported earlier, to evaluate the temperature dependences of K-s,2(o) for the dipeptides in the temperature range 15 to 35 degrees C. The K-s,2(o), values for all the dipeptides are nega tive and increase (become more positive) with an increase in temperatu re. The slopes of the temperature dependences of K-s,2(o) for the dipe ptides with typically hydrophobic side-chains are significantly larger than those for dipeptides with hydrophilic side-chains.