Narrowing of Protein NMR Spectral Lines Broadened by Chemical Exchange

Ying Li, Arthur G. Palmer
2010 Journal of the American Chemical Society  
NMR techniques for characterizing chemical exchange phenomena have found widespread use in studies of protein and nucleic acid dynamics, which are closely linked to biological functions, including enzyme catalysis, ligand binding, and allosteric regulation. 1,2 However, chemical exchange on microsecond to millisecond time scales broadens spectral lines, with deleterious effects on resolution and sensitivity. We present a multipulse method for reducing chemical exchange broadening during the
more » ... uency-encoding periods of liquid-state multidimensional NMR experiments. Enhanced resolution and sensitivity are demonstrated for exchange-broadened 15 N resonances of the protein ribonuclease A (RNase A).
doi:10.1021/ja103251h pmid:20550111 pmcid:PMC2921271 fatcat:tgzkjh3q5rhinin6kxeajesara