Impact of distal mutations on the ... | Article | H1 Connect

Dihydrofolate reductase from Escherichia coli is a preferred model system for studying the dynamics across the protein in the chemical step catalyzed by this enzyme because it is a small monomeric enzyme, has no metals or S-S bonds, and folds reversibly. This article, together with {1-4}, presents molecular calculations of dihydrofolate reductase from Escherichia coli, along with bioinformatics statistics of the enzyme from various organisms, that predict that several residues in the enzyme’s active site as well as several residues remote from the active site are dynamically and genetically coupled to the catalyzed reaction. This Recommendation is of an article referenced in an F1000 Faculty Review also written by Amnon Kohen.