A free-energy perturbation study of the binding of methotrexate to mutants of dihydrofolate reductase.
The importance of hydrophobic residues to the binding of methotrexate in the active site of dihydrofolate reductase (EC 1.5.1.3) was examined by a free-energy perturbation method. The replacement of a strictly conserved residue, Phe-31, by tyrosine or valine costs 1.8 and 5.1 kcal/mol, respectively,...
שמור ב:
| הוצא לאור ב: | Proc Natl Acad Sci U S A |
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| Principais autores: | , |
| פורמט: | Artigo |
| שפה: | Inglês |
| יצא לאור: |
National Academy of Sciences
1988
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| נושאים: | |
| גישה מקוונת: | https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC282785/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/3200837/ https://ncbi.nlm.nih.govhttps://doi.org/10.1073/pnas.85.24.9519 |
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