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Effects of denaturants at low concentrations on the reversible denaturation of staphylococcal nuclease

✍ Scribed by David Shortle; Alan K. Meeker; Sandra L. Gerring

Book ID
115708081
Publisher
Elsevier Science
Year
1989
Tongue
English
Weight
998 KB
Volume
272
Category
Article
ISSN
0003-9861

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πŸ“œ SIMILAR VOLUMES

Thermodynamics of staphylococcal nucleas
Thermodynamics of staphylococcal nuclease denaturation. I. The acid-denatured state
✍ 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

Thermodynamics of staphylococcal nucleas
Thermodynamics of staphylococcal nuclease denaturation. II. The A-state
✍ 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