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Cross-relaxation bottleneck in water–lysozyme proton magnetization exchange

✍ Scribed by J. F. Kakule; A. R. Sharp; L. J. Schreiner; R. T. Thompson; T. Kupka; R. Holly; H. Peemoeller

Publisher: Wiley (John Wiley & Sons)
Year: 2006
Tongue: English
Weight: 215 KB
Volume: 83
Category: Article
ISSN: 0006-3525
DOI: 10.1002/bip.20522

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✦ Synopsis

Abstract

The proton spin‐lattice relaxation parameters in natural and deuterated lysozyme solutions have been measured as a function of temperature (0–50°C). The variation of the apparent magnitudes of the water proton magnetizations in the solutions with temperature indicates that magnetic coupling mixes protein and water proton magnetizations. The results are consistent with an exchange cross‐relaxation model (Hills, B. P., Mol Phys 1992, 76, 489–508) in which the cross‐relaxation acts between the labile and nonlabile protons, rather than between water and protein protons. Although this cross‐relaxation pathway clearly affects the observed magnetization fractions in this protein solution, its influence on the relaxation rates is less apparent. © 2006 Wiley Periodicals, Inc. Biopolymers 83: 11–19, 2006

This article was originally published online as an accepted preprint. The “Published Online” date corresponds to the preprint version. You can request a copy of the preprint by emailing the Biopolymers editorial office at [email protected]

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