Paper Information

Journal:   JOURNAL OF THE IRANIAN CHEMICAL SOCIETY(JICS)   December 2004 , Volume 1 , Number 2; Page(s) 99 To 105.
 
Paper: 

ON THE ESTIMATION OF STABILITY PARAMETERS FROM HEAT-INDUCED CONFORMATIONAL TRANSITION CURVES OF PROTEINS

 
 
Author(s):  AHMAD F.*
 
* Jamia Nagar, New Delhi,India
 
Abstract: 
A method is suggested to determine valid and authentic values of thermodynamic stability parameters of proteins from their heat-induced conformational transition curves. We show (a) that the estimate of DHmvan, the enthalpy change on denaturation at Tm, the midpoint of denaturation, is significantly less than DHmcal, the value obtained by the calorimetric measurements, if the analysis of the conformational transition curve uses the conventional method which assumes a linear temperature-dependence of the pre- and post-transition baselines; and (b) that there exists an excellent agreement between DHmvan and DHmcal values of proteins, if the analysis of thermal denaturation curves assumes that the temperature-dependence of pre- and post-transition baselines is described by a parabolic function. The latter analysis is supported by our observations that the temperature-dependencies of the absorption and circular dichroism properties of protein groups are indeed nonlinear. It is observed that the estimate of DCp, the constant-pressure heat capacity change is independent of the model used to describe the temperature-dependence of the pre- and post-transition baselines. An important conclusion is that for proteins which exhibit a two-state character, all stability parameters are measured with the same error as that observed with a calorimeter.
 
Keyword(s): PROTEIN STABILITY, THERMAL DENATURATION, VANT HOFF ANALYSIS, ENTHALPY CHANGE, HEAT CAPACITY CHANGE, GIBBS ENERGY CHANGE, RIBONUCLEASE, LYSOZYME
 
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