DSC STUDY OF THE THERMAL-STABILITY OF S-PROTEIN AND S-PEPTIDE S-PROTEIN COMPLEXES/

Citation
G. Graziano et al., DSC STUDY OF THE THERMAL-STABILITY OF S-PROTEIN AND S-PEPTIDE S-PROTEIN COMPLEXES/, Biochemistry, 35(41), 1996, pp. 13386-13392
Citations number
56
Language
INGLESE
art.tipo
Article
Categorie Soggetti
Biology
Journal title
Biochemistry → ACNP
ISSN journal
0006-2960
Volume
35
Issue
41
Year of publication
1996
Pages
13386 - 13392
Database
ISI
SICI code
0006-2960(1996)35:41<13386:DSOTTO>2.0.ZU;2-3
Abstract
The thermal denaturation of S-protein is investigated at pH 7.0 by mea ns of DSC measurements. The process is reversible and can be assimilat ed to a two-state transition, The low values of denaturation temperatu re and enthalpy, between 38.5 and 40.0 degrees C and 165 and 180 kJ mo l(-1), respectively, demonstrate that the loss of S-peptide strongly d ecreases the structural stability. The interaction between S-peptide a nd S-protein is thermodynamically characterized, at pH 7.0, by studyin g the thermal stability of S-peptide/S-protein complexes at different molar ratios. A two-dimensional nonlinear regression analysis of the e xcess heat capacity surface as a function of temperature and S-peptide concentration enables us to determine the thermodynamic parameters of binding equilibrium. The values obtained are K-b(38.6 degrees C) = (1 .10 +/- 0.15) x 10(6) M(-1). Delta(b)H(38.6 degrees C) = (-185 +/- 10) kJ mol(-1), and Delta(b)C(p) = (-3.5 +/- 0.5) kJ K-1 mol(-1). These f igures result in satisfactory agreement with literature values.