Improved resolution in three-dimensional constant-time triple resonance NMR spectroscopy of proteins.
Two new protocols for the three-dimensional, triple resonance, constant-time HCA(CO)N NMR experiment are presented that significantly increase the experimental resolution attainable in the C alpha frequency dimension. Experimental verification of the new experiments is provided by spectra of the IIA domain of glucose permease from Bacillus subtilis.
Palmer
A G
AG
Department of Molecular Biology, Scripps Research Institute, La Jolla, CA 92037.
Fairbrother
W J
WJ
Cavanagh
J
J
Wright
P E
PE
Rance
M
M
D000595:Amino Acid Sequence; D001412:Bacillus subtilis / Q000201:enzymology; D009682:Magnetic Resonance Spectroscopy / Q000379:methods*; D008433:Mathematics; D010731:Phosphoenolpyruvate Sugar Phosphotransferase System / Q000737:chemistry*; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry*; D013997:Time Factors
D011506:Proteins; D010731:Phosphoenolpyruvate Sugar Phosphotransferase System; C031629:phosphoenolpyruvate-glucose phosphotransferase