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Cold Denaturation of Staphylococcal Nuclease

✍ Scribed by Yuri V. Griko, Peter L. Privalov, Julian M. Sturtevant and Sergey Yu. Venyaminov


Book ID
123635529
Publisher
National Academy of Sciences
Year
1988
Tongue
English
Weight
616 KB
Volume
85
Category
Article
ISSN
0027-8424

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πŸ“œ SIMILAR VOLUMES


Thermodynamics of staphylococcal nucleas
✍ John H. Carra; Elizabeth A. Anderson; Peter L. Privalov πŸ“‚ Article πŸ“… 2008 πŸ› Cold Spring Harbor Laboratory Press 🌐 English βš– 776 KB

## Abstract Staphylococcal nuclease, at low pH and in the presence of high salt concentrations, has previously been proposed to exist in a partially folded or molten globule form called the β€œA‐state” (Fink et al., 1993, __Protein Sci 2__:1155–1160). We have found that the A‐state of nuclease at pH

Thermodynamics of staphylococcal nucleas
✍ John H. Carra; Elizabeth A. Anderson; Peter L. Privalov πŸ“‚ Article πŸ“… 2008 πŸ› Cold Spring Harbor Laboratory Press 🌐 English βš– 831 KB

## Abstract Using high‐sensitivity differential scanning calorimetry, we reexamined the thermodynamics of denaturation of staphylococcal nuclease. The denaturational changes in enthalpy and heat capacity were found to be functions of both temperature and pH. The denatured state of staphylococcal nu

Thermal denaturation of staphylococcal n
✍ Calderon, Reyna O.; Stolowich, Neal J.; Gerlt, John A.; Sturtevant, Julian M. πŸ“‚ Article πŸ“… 1985 πŸ› American Chemical Society 🌐 English βš– 635 KB
Guanidine hydrochloride denaturation stu
✍ David Shortle πŸ“‚ Article πŸ“… 1986 πŸ› John Wiley and Sons 🌐 English βš– 581 KB

Several mutant forms of staphylococcal nuclease with one or two defined amino acid substitutions have been purified, and the effects of the altered amino acid sequence on the stability of the folded conformation have been analyzed by guanidine hydrochloride denaturation. Two nuc-mutations, which gre