Detection of intramolecular interactions of lysyl and N-terminal amino groups of reductively methylated proteins by /sup 13/C nuclear magnetic resonance

Journal Article · Wed Oct 01 04:00:00 EDT 1980 · Biophys. J.; (United States)

DOI:https://doi.org/10.1016/S0006-3495(80)84928-9· OSTI ID:6796262

Jentoft, J E; Dearborn, D G; Gerken, T A; Jentoft, N

Detailed information on the intramolecular interactions of protein amino groups has been largely unobtainable except to a limited extent from crystallographic studies. Reductive methylation with NaCNBH/sub 3/ and (/sup 13/C)-formaldehyde introduces a specific probe for /sup 13/C nuclear magnetic resonance (NMR) investigation of protein amino groups. We have shown that the chemical shifts of /sup 13/C-enriched dimethylamino groups are sensitive to the environment and degree of protonation of the amino group, and we have demonstrated that the pK of the dimethylamino groups are very similar to those of unmodified amino groups.

• Research Organization: Case Western Reserve Univ., Cleveland, OH
• OSTI ID: 6796262
• Journal Information: Biophys. J.; (United States), Journal Name: Biophys. J.; (United States) Vol. 32:1; ISSN BIOJA
• Country of Publication: United States
• Language: English

Related Subjects

550200* -- Biochemistry
59 BASIC BIOLOGICAL SCIENCES
BIOCHEMISTRY
CARBON 13
CARBON ISOTOPES
CHEMICAL REACTIONS
CHEMICAL SHIFT
CHEMISTRY
ENZYMES
ESTERASES
EVEN-ODD NUCLEI
GLYCOSYL HYDROLASES
HYDROLASES
INTERMOLECULAR FORCES
ISOTOPES
LIGHT NUCLEI
LYSOZYME
MAGNETIC RESONANCE
METHYLATION
NMR SPECTRA
NUCLEAR MAGNETIC RESONANCE
NUCLEI
O-GLYCOSYL HYDROLASES
PH VALUE
PHOSPHODIESTERASES
RESONANCE
RNA-ASE
SPECTRA
STABLE ISOTOPES
STRUCTURAL CHEMICAL ANALYSIS