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Correlated conformational fluctuations during enzymatic catalysis: Implications for catalytic rate enhancement
Correlated enzymatic conformational fluctuations are shown to contribute to the rate of enhancement achieved during catalysis. Cytidine deaminase serves as a model system. Crystallographic temperature factor data for this enzyme complexed with substrate analog, transition-state analog, and product a...
Tallennettuna:
| Päätekijät: | , , , |
|---|---|
| Aineistotyyppi: | Artigo |
| Kieli: | Inglês |
| Julkaistu: |
Cold Spring Harbor Laboratory Press
2001
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| Aiheet: | |
| Linkit: | https://ncbi.nlm.nih.gov/pmc/articles/PMC2374110/ https://ncbi.nlm.nih.gov/pubmed/11420434 |
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