Dynamics Investigation of the Cytochrome P450cam Active Site Mutant Thr252ALA
โ Scribed by Reyles, Jonathan; Miao, Yinglong; Baudry, Jerome; Smith, Jeremy C.
- Book ID
- 121920753
- Publisher
- Biophysical Society
- Year
- 2011
- Tongue
- English
- Weight
- 59 KB
- Volume
- 100
- Category
- Article
- ISSN
- 0006-3495
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๐ SIMILAR VOLUMES
Energetically favorable water binding sites in the substrate pocket ofcytochrome P450-cam have been predicted by a molecular mechanics method. Binding sites corresponding to all the experimentally observed water sites in this region of the enzyme were located. The calculations also indicate the pres
Hydration of protein cavities influences protein stability, dynamics, and function. Protein active sites usually contain water molecules that, upon ligand binding, are either displaced into bulk solvent or retained to mediate protein-ligand interactions. The contribution of water molecules to ligand