Effects of denaturants and substitutions of hydrophobic residues on backbone dynamics of denatured staphylococcal nuclease
โ Scribed by Satoshi Ohnishi; David Shortle
- Book ID
- 111752170
- Publisher
- Cold Spring Harbor Laboratory Press
- Year
- 2003
- Tongue
- English
- Weight
- 201 KB
- Volume
- 12
- Category
- Article
- ISSN
- 0961-8368
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๐ SIMILAR VOLUMES
Recent work has suggested that changes in NMR order parameters may quantitatively reflect changes in the conformational entropy of a protein ensemble. The extent of the mathematical relationship between local entropy changes as seen by NMR order parameters and the full protein entropy change is a co
The thermal denaturations of five revertant h repressors containing single amino acid substitutions in their N-terminal domains have been studied by differential scanning calorimetry. Two substitutions slightly decrease stability, and the remaining three render the protein more stable than wild type