Cold Denaturation of Staphylococcal Nuclease

Denaturation of staphylococcal nuclease was studied in a temperature range from -7 to 70 degrees C by scanning microcalorimetry and spectropolarimetry. It was found that the native protein is maximally stable at about 20 degrees C and is denatured upon heating and cooling from this temperature. The...

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Bibliographic Details
Published in:Proceedings of the National Academy of Sciences - PNAS 1988-05, Vol.85 (10), p.3343-3347
Main Authors: Griko, Yuri V., Privalov, Peter L., Sturtevant, Julian M., Sergey Yu. Venyaminov
Format: Article
Language:English
Subjects:
Acetates
Analytical, structural and metabolic biochemistry
Biological and medical sciences
Calorimetry
Cold Temperature
Enthalpy
Enzymes and enzyme inhibitors
Fundamental and applied biological sciences. Psychology
Heat
Hydrolases
Low temperature
Micrococcal Nuclease
nuclease
Protein Denaturation
Proteins
Specific heat
Temperature dependence
Temperature effects
Transition temperature
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Summary:Denaturation of staphylococcal nuclease was studied in a temperature range from -7 to 70 degrees C by scanning microcalorimetry and spectropolarimetry. It was found that the native protein is maximally stable at about 20 degrees C and is denatured upon heating and cooling from this temperature. The heat and cold denaturation processes are approximated rather well by a two-state transition showing that the molecule is composed of a single cooperative system. The main difference between these two processes is in the sign of the enthalpy and entropy of denaturation: whereas the heat denaturation proceeds with increases in the enthalpy and entropy, the cold denaturation proceeds with decreases in both quantities. The inversion of the enthalpy sign occurs at about 15 degrees C in an acetate buffer, but this temperature can be raised by addition of urea to the solvent.
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.85.10.3343