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Elimination of spin diffusion effects in saturation transfer experiments: application to hydrogen exchange in proteins
Author(s) -
Jensen Malene Ringkjøbing,
Kristensen Søren M.,
Led Jens J.
Publication year - 2007
Publication title -
magnetic resonance in chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.483
H-Index - 72
eISSN - 1097-458X
pISSN - 0749-1581
DOI - 10.1002/mrc.1955
Subject(s) - chemistry , saturation (graph theory) , diffusion , chemical physics , magnetization transfer , hydrogen , analytical chemistry (journal) , thermodynamics , chromatography , organic chemistry , medicine , physics , mathematics , radiology , combinatorics , magnetic resonance imaging
The NMR saturation transfer experiment is widely used to characterize exchange processes in proteins that take place on the ms‐s timescale. However, spin diffusion effects are inherently associated with the saturation transfer experiment and may overshadow the effect of the exchange processes of interest. As shown here, the effects from spin diffusion and exchange processes can be separated by varying the field strength of the saturation pulse, thereby allowing correct exchange rates to be obtained. The method is demonstrated using the hydrogen exchange process in the protein Escherichia coli thioredoxin as an example. Copyright © 2007 John Wiley & Sons, Ltd.

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