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/sup 13/C NMR evidence of the slow exchange of tryptophans in dihydrofolate reductase between stable conformations

Journal Article · · Biochem. Biophys. Res. Commun.; (United States)
/sup 13/C NMR spectra are reported for dihydrofolate reductase of Streptococcus faecium labeled with (..gamma..-/sup 13/C)tryptophan. Two of the four tryptophans generate unusual resonances indicating slow exchange of the residues between alternative stable conformations. Since 3', 5'-dichloromethotrexate sharpens two of the resonances, it apparently locks the corresponding residues into one conformation.
OSTI ID:
5374346
Journal Information:
Biochem. Biophys. Res. Commun.; (United States), Journal Name: Biochem. Biophys. Res. Commun.; (United States) Vol. 86:3; ISSN BBRCA
Country of Publication:
United States
Language:
English