Stabilization of Charges and Protonation States in the Active Site of the Protein Tyrosine Phosphatases: A Computational Study †
✍ Scribed by Dillet, Valérie; Van Etten, Robert L.; Bashford, Donald
- Book ID
- 126206662
- Publisher
- American Chemical Society
- Year
- 2000
- Tongue
- English
- Weight
- 212 KB
- Volume
- 104
- Category
- Article
- ISSN
- 0022-3654
No coin nor oath required. For personal study only.
📜 SIMILAR VOLUMES
Molecular dynamics simulation of the Michaelis complex, phospho-enzyme intermediate, and the wild-type and C12S mutant have been carried out to examine hydrogen-bonding interactions in the active site of the bovine low molecular weight protein-tyrosine phosphatase (BPTP). It was found that the S γ a
The oxidation state of the cysteine residue at the active site of human protein tyrosine phosphatase (PTP-1B) greatly affects its enzymatic activity. We wished to examine peroxide-treated preparations for modifications of this enzyme with electrospray mass spectrometry in order to determine the loca