Carbonyl 13C-detect solution-state protein NMR experiments to circumvent amide-solvent exchange broadening: Application to β2-microglobulin.
The 15N-1H heteronuclear single-quantum correlation (HSQC) technique in protein NMR spectroscopy suffers from line-broadening effects, such as chemical exchange of labile protons with solvent, and exchange broadening for residues undergoing conformational dynamics. The amide resonance of β2-microglobulin residue S88 is not observed in the HSQC spectrum but can be obtained through 13C-detect experiments that circumvent the problem of amide-solvent exchange broadening. Line broadening of S88 resonance beyond detection in the HSQC spectrum is not attributed to conformational exchange but rather to solvent exchange occurring on the order of ~103 s-1.
['Yoshimura|Yuichi|Y|', 'So|Masatomo|M|', 'Miyanoiri|Yohei|Y|']
D000577:Amides D002247:Carbon Isotopes D011487:Protein Conformation D066244:Proton Magnetic Resonance Spectroscopy D012997:Solvents D001613:beta 2-Microglobulin
(13)C-detect NMR spectroscopy Hydrogen exchange NMR relaxation β(2)-microglobulin