The entropy cost of protein association.
作者： Atsuo Tamura , Peter L Privalov
关键词: Calorimetry 、 Order of magnitude 、 Circular dichroism 、 Entropy (information theory) 、 Protein folding 、 Nuclear magnetic resonance spectroscopy 、 Chemistry 、 Subtilisin 、 Dimer 、 Thermodynamics
摘要: The temperature induced unfolding/dissociation of the dimeric subtilisin inhibitor from Streptomyces and its mutant D83C having an S-S crosslink between subunits has been studied calorimetrically. Comparison entropies measured at different concentrations dimer showed that entropy cost crosslinking is small. Its value standard concentration 1 M order -(5+/-4) cal/K.mol, i.e. it more than one magnitude smaller values translational calculated on base statistical thermodynamics, using in particular Sackur-Tetrode equation, close to cratic suggested by classical mixing theory.
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