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| - Separating Degenerate 1H Transitions in Methyl Group Probesfor Single-Quantum 1H-CPMG Relaxation Dispersion NMRSpectroscopy
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| - A relaxation dispersion pulse scheme is presented for quantifying chemical exchange processesin proteins that exploits 1H chemical shifts as probes of changes in conformation. The experiment selects1H single-quantum magnetization from the I = 1/2 manifolds of the methyl group, which behave like AXspin systems, while suppressing coherences that derive from the 3/2 manifold that are extremely sensitiveto pulse imperfections and that would otherwise severely compromise the accuracy of the experiment.The utility of the sequence is first demonstrated with an application to a protein system that is known notto undergo chemical exchange and flat dispersion profiles are obtained. Subsequently, the methodology isapplied to study the folding of a G48M mutant of the Fyn SH3 domain that has been shown previously toundergo exchange between folded and unfolded states on the millisecond time scale.
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