Abstract
Oxygen-17 and deuteron longitudinal and transverse spin relaxation rates from aqueous protein solutions (mainly lysozyme and haemocyanin) have been measured as a function of temperature, pH and resonance frequency. A detailed comparison of the 17O and 2H data demonstrates that 2H relaxation has a dominant contribution which is not seen by 17O. This contribution is, at least partly, due to deuteron exchange with ionizable groups on the protein. Furthermore, we refute two widespread beliefs about solvent spin relaxation in protein solutions, namely that the discrete-exchange model leads to interpretational inconsistencies and that the low-frequency dispersion always reflects protein reorientation.
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Schedule a callMore From: Journal of the Chemical Society, Faraday Transactions 1: Physical Chemistry in Condensed Phases
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