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Literature summary for 1.5.1.3 extracted from

  • Thielges, M.C.; Case, D.A.; Romesberg, F.E.
    Carbon-deuterium bonds as probes of dihydrofolate reductase (2008), J. Am. Chem. Soc., 130, 6597-6603.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

Crystallization (Comment) Organism
use of carbon-deuterium bonds as probes of proteins. The stretching absorption frequency of (methyl-d3) methionine carbon-deuterium bonds shows an approximately linear dependence on solvent dielectric. Characterization of the IR absorptions at residues Met16 and Met20, within the catalytically important Met20 loop, and Met42, which is located within the hydrophobic core of the enzyme. The carbon-deuterium bonds tare sensitive to their local protein environment and dihydrofolate reductase is electrostatically and dynamically heterogeneous Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
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