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Active-site residues move independently from the rest of the protein in a 200 ns molecular dynamics simulation of cytochrome P450 CYP119
The conformational dynamics of cytochrome P450 enzymes are critical to their catalytic activity. In this study, the correlated motion between residues in a 200ns molecular dynamics trajectory of the thermophilic CYP119 was analyzed to parse out conformational relationships. Residues that are structu...
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| Główni autorzy: | , , , |
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| Format: | Artigo |
| Język: | Inglês |
| Wydane: |
2011
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| Hasła przedmiotowe: | |
| Dostęp online: | https://ncbi.nlm.nih.gov/pmc/articles/PMC3085956/ https://ncbi.nlm.nih.gov/pubmed/21356195 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1016/j.abb.2011.02.020 |
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