𝔖 Bobbio Scriptorium
✦   LIBER   ✦

Thermal denaturation of staphylococcal nuclease

✍ Scribed by Calderon, Reyna O.; Stolowich, Neal J.; Gerlt, John A.; Sturtevant, Julian M.

Book ID
125994569
Publisher
American Chemical Society
Year
1985
Tongue
English
Weight
635 KB
Volume
24
Category
Article
ISSN
0006-2960

No coin nor oath required. For personal study only.

πŸ“œ SIMILAR VOLUMES

Cold Denaturation of Staphylococcal Nucl
Cold Denaturation of Staphylococcal Nuclease
✍ Yuri V. Griko, Peter L. Privalov, Julian M. Sturtevant and Sergey Yu. Venyaminov πŸ“‚ Article πŸ“… 1988 πŸ› National Academy of Sciences 🌐 English βš– 616 KB
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