A 1H-15N NMR study of human c-Ha-ras protein: biosynthetic incorporation of 15N-labeled amino acids.
A 1H-15N NMR study was performed on the GDP-bound form of a truncated human c-Ha-ras oncogene product (171 amino acid residues). Resonance cross peaks of the backbone amide 1H-15N nuclei of a uniformly 15N-labeled protein were observed with heteronuclear single-quantum coherence spectroscopy (HSQC). In order to resolve overlapping cross peaks, selective 15N-labeling of one or two types of amino acid residues (Ala, Arg, Asx, Glx, Gly, His, Ile, Leu, Lys, Met, Phe, Ser, Thr, Tyr and/or Val) was carried out using appropriate E. coli mutant strains. By this procedure, all the backbone 1H-15N cross peaks were classified into amino acid types.
Yamasaki
K
K
Department of Biophysics and Biochemistry, Faculty of Science, University of Tokyo, Japan.
Muto
Y
Y
Ito
Y
Y
Wälchli
M
M
Miyazawa
T
T
Nishimura
S
S
Yokoyama
S
S
D000596:Amino Acids / Q000378:metabolism; D003001:Cloning, Molecular; D004926:Escherichia coli / Q000235:genetics; D005813:Genes, Synthetic; D011905:Genes, ras; D006801:Humans; D006859:Hydrogen; D007553:Isotope Labeling / Q000379:methods; D009682:Magnetic Resonance Spectroscopy / Q000379:methods; D009587:Nitrogen Isotopes; D011487:Protein Conformation; D016283:Proto-Oncogene Proteins p21(ras) / Q000096:biosynthesis / Q000737:chemistry* / Q000235:genetics; D011994:Recombinant Proteins / Q000096:biosynthesis / Q000235:genetics
D000596:Amino Acids; D009587:Nitrogen Isotopes; D011994:Recombinant Proteins; D006859:Hydrogen; C501009:HRAS protein, human; D016283:Proto-Oncogene Proteins p21(ras)