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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,...

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Bibliografske podrobnosti
Main Authors: Singh, U C, Benkovic, S J
Format: Artigo
Jezik:Inglês
Izdano: 1988
Teme:
Online dostop:https://ncbi.nlm.nih.gov/pmc/articles/PMC282785/
https://ncbi.nlm.nih.gov/pubmed/3200837
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