Catalytic Site pKa Values of Aspartic, Cysteine, and Serine Proteases: Constant pH MD Simulations
| Autor: | Ursula Kahler, Johannes Kraml, Klaus R. Liedl, Anna S. Kamenik, Florian Hofer |
|---|---|
| Rok vydání: | 2020 |
| Předmět: |
chemistry.chemical_classification
Proteases 010304 chemical physics biology Stereochemistry General Chemical Engineering Active site Titratable acid Protonation General Chemistry Library and Information Sciences 01 natural sciences 0104 chemical sciences Computer Science Applications Catalysis Serine 010404 medicinal & biomolecular chemistry Enzyme chemistry 0103 physical sciences biology.protein sense organs Cysteine |
| Zdroj: | Journal of Chemical Information and Modeling. 60:3030-3042 |
| ISSN: | 1549-960X 1549-9596 |
| DOI: | 10.1021/acs.jcim.0c00190 |
| Popis: | Enzymatic function and activity of proteases is closely controlled by the pH value. The protonation states of titratable residues in the active site react to changes in the pH value, according to t... |
| Databáze: | OpenAIRE |
| Externí odkaz: |
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