Dipolar dynamic frequency shifts in multiple-quantum spectra of methyl groups in proteins: correlation with side-chain motion

Small deviations from the expected relative positions of multiplet components in double‐ and zero‐quantum 1H‐13C methyl correlation maps have been observed in spectra recorded on a 7‐kDa protein. These dynamic frequency shifts (DFS) are the result of dipolar cross‐correlations that derive from field...

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Veröffentlicht in:	Magnetic resonance in chemistry 2006-07, Vol.44 (S1), p.S122-S129
Hauptverfasser:	Tugarinov, Vitali, Ollerenshaw, Jason E., Kay, Lewis E.
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acids - chemistry Carbon Isotopes cross-correlated relaxation dynamic frequency shift Isotope Labeling methyl group Methylation Models, Chemical multiple-quantum spectroscopy Nuclear Magnetic Resonance, Biomolecular Proteins - chemistry Protons Quantum Theory side-chain order parameter
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