Globular proteins thermodynamic parameters

Thermodynamic Parameters of Denaturation of Compact Globular Proteins with Average Molecular Weight ... 

Prompers and Briischweiler showed by quasiharmonic analysis that the conformational partition function of a globular protein sampled on the ns time scale can be factorized in good approximation into purely reorientational part, which determines heteronuclear NMR spin relaxation, and a remaining part that includes other types of intramolecular motions. Thus a thermodynamic interpretation of NMR relaxation parameters in proteins in the presence of motional correlations can be given. 

The biophysical characterization of globular proteins will almost always include some type of study of the unfolding of protein to obtain thermodynamic parameters. The basic idea is that a transition between a native and unfolded state, induced by temperature, pH, or denaturant concentration, can serve as a standard reaction for obtaining a thermodynamic measure of the stability of the native state. For example, the free energy change for the unfolding reaction can be used to compare the stability of a set of mutant forms of a protein (1-4). 

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