作者: C. A. Royer , R. Winter
DOI: 10.1007/978-3-540-88787-4_9
关键词: Staphylococcal Nuclease 、 Protein thermodynamics 、 Solvent 、 Calorimetry 、 Compressibility 、 Small field 、 Enthalpy 、 Chemistry 、 Thermodynamics 、 Protein structure
摘要: Walter Kauzmann stated in a review of protein thermodynamics that “volume and enthalpy changes are equally fundamental properties the unfolding process, no model can be considered acceptable unless it accounts for entire thermodynamic behaviour” (Nature 325:763–764, 1987). While basis pressure effects has been known some time, molecular mechanisms have remained rather mysterious. We, others small field on structure stability, attempted since time to clarify physical volume accompany conformational transitions, hence explain proteins. The combination many years work system, staphylococcal nuclease its large numbers site-specific mutants, new perturbation calorimetry approach provided first qualitative understanding ΔV unfolding, quantitative which remains goal current work.