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Active Site Hydrophobic Residues Impact Hydrogen Tunneling Differently in a Thermophilic Alcohol Dehydrogenase at Optimal vs. Non-Optimal Temperatures
A growing body of data suggests that protein motion plays an important role in enzyme catalysis. Two highly conserved hydrophobic active site residues in the cofactor-binding pocket of ht-ADH (Leu176 and V260) have been mutated to a series of hydrophobic side chains of smaller size, as well as one d...
Tallennettuna:
| Päätekijät: | , , , , |
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| Aineistotyyppi: | Artigo |
| Kieli: | Inglês |
| Julkaistu: |
2012
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| Aiheet: | |
| Linkit: | https://ncbi.nlm.nih.gov/pmc/articles/PMC3498984/ https://ncbi.nlm.nih.gov/pubmed/22568562 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1021/bi3001352 |
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