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

Copyright 2006 John Wiley & Sons, Ltd.

Bibliographische Detailangaben
Veröffentlicht in:Magnetic resonance in chemistry : MRC. - 1985. - 44 Spec No(2006) vom: 01. Juli, Seite S122-9
1. Verfasser: Tugarinov, Vitali (VerfasserIn)
Weitere Verfasser: Ollerenshaw, Jason E, Kay, Lewis E
Format: Aufsatz
Sprache:English
Veröffentlicht: 2006
Zugriff auf das übergeordnete Werk:Magnetic resonance in chemistry : MRC
Schlagworte:Journal Article Research Support, Non-U.S. Gov't Amino Acids Carbon Isotopes Proteins Protons
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520 |a 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 fields produced by the spins within the methyl groups. The shifts have been quantified and compared with values calculated from a Redfield analysis. Good agreement is noted between the signs of the predicted and experimentally observed relative shifts of lines in both F1 and F2 dimensions of spectra, as well as between the magnitudes of the calculated and observed shifts in the F2 (1H) dimension. The experimental DFS values show a reasonable correlation with 2H relaxation-derived measures of methyl side-chain dynamics, as expected from theory. This suggests that in cases where such shifts can be quantified, they can serve as qualitative measures of motion 
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