A study of the hydration of ribonuclease A using densitometry: Effect of the protein hydrophobicity and polarity
โ Scribed by Sirotkin, Vladimir A.; Khadiullina, Aigul V.
- Book ID
- 122267373
- Publisher
- Elsevier Science
- Year
- 2014
- Tongue
- English
- Weight
- 806 KB
- Volume
- 603
- Category
- Article
- ISSN
- 0009-2614
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๐ SIMILAR VOLUMES
The use of a linear relationship between free energy of hydrophobic hydration and solvent-accessible apolar surface area has been helpful in interpreting the thermodynamics of biological macromolecules. However, a recent study (Y.-K. Cheng, P. J. Rossky, Nature 1998, Vol. 392, pp. 696-699) has estab
## Abstract Enzymes with ribonucleolytic activity play a pivotal role in gene expression and cellular homeostasis by altering the levels of cellular RNA. Ribonuclease A has been the most well studied of such enzymes whose histidine residues (His^12^ and His^119^) play a crucial role in the catalyti