/sup 13/C nuclear magnetic resonance study of the interaction of ligands with arginine residues in dihydrofolate reductase

Journal Article · Sat Jan 01 04:00:00 EST 1977 · Biochem. Biophys. Res. Commun.; (United States)

DOI:https://doi.org/10.1016/0006-291X(77)91684-9· OSTI ID:6389745

Cocco, L ^[1]; Blakley, R L; Walker, T E; London, R E

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1. Univ. of Iowa, Iowa City

/sup 13/C NMR spectra of Streptococcus faecium dihydrofolate reductase containing (/sup 13/C-guanidino) arginine and ligand complexes with the labeled enzyme are reported. The spectrum of the native enzyme shows 5 well-resolved resonances (the enzyme contains 8 Arg) with a chemical shift range of 1.2 ppM. Addition of ligands to the enzyme produces distinct changes in the enzyme spectrum, and demonstrates that /sup 13/C NMR of labeled protein can be used in studies of protein-ligand interactions. An example of the use of /sup 13/C-depleted material is also presented.

• OSTI ID: 6389745
• Journal Information: Biochem. Biophys. Res. Commun.; (United States), Journal Name: Biochem. Biophys. Res. Commun.; (United States) Vol. 76:1; ISSN BBRCA
• Country of Publication: United States
• Language: English

Related Subjects

37 INORGANIC, ORGANIC, PHYSICAL, AND ANALYTICAL CHEMISTRY
400301* -- Organic Chemistry-- Chemical & Physicochemical Properties-- (-1987)
AMINO ACIDS
ARGININE
CARBON 13
CARBON ISOTOPES
CARBOXYLIC ACIDS
CHEMICAL REACTIONS
ENZYMES
EVEN-ODD NUCLEI
ISOTOPES
LABELLED COMPOUNDS
LIGANDS
LIGHT NUCLEI
MAGNETIC RESONANCE
NUCLEAR MAGNETIC RESONANCE
NUCLEI
ORGANIC ACIDS
ORGANIC COMPOUNDS
OXIDOREDUCTASES
RESONANCE
STABLE ISOTOPES