Thermal denaturation of staphylococcal nuclease

The fully reversible thermal denaturation of staphylococcal nuclease in the absence and presence of Ca2+ and/or thymidine 3',5'-diphosphate (pdTp) from pH 4 to 8 has been studied by high-sensitivity differential scanning calorimetry. In the absence of ligands, the denaturation is accompani...

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Veröffentlicht in:	Biochemistry (Easton) 1985-10, Vol.24 (22), p.6044-6049
Hauptverfasser:	Calderon, Reyna O, Stolowich, Neal J, Gerlt, John A, Sturtevant, Julian M
Format:	Artikel
Sprache:	eng
Schlagworte:	Analytical, structural and metabolic biochemistry Biological and medical sciences Calorimetry Enzymes and enzyme inhibitors Escherichia coli - enzymology Fundamental and applied biological sciences. Psychology Hydrogen-Ion Concentration Hydrolases Kinetics Ligands Micrococcal Nuclease - metabolism Protein Denaturation Thermodynamics
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