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Theoretical reason for the lack of influence of 1H–14N cross-relaxation on the water proton T 1 NMRD profile in slow tumbling proteins
Umeå University, Faculty of Science and Technology, Department of Chemistry.
2012 (English)In: Molecular Physics, ISSN 0026-8976, E-ISSN 1362-3028, Vol. 110, no 18, 2251-2255 p.Article in journal (Refereed) Published
Abstract [en]

For immobilized protein the water proton T 1-NMRD profile displays three enhanced relaxation peaks (QP). For slow tumbling proteins these relaxation peaks are not experimentally observed. However, the theoretically determined QP effect on the amide proton T 1-NMRD profile displays a distorted Lorentzian dispersion profile. The question arises as to whether there is also a distortion of the water-proton T 1-NMRD profile due to QP. The model of Sunde and Halle [J. Magn. Reson. 203, 257 (2010)] predicts a decreasing QP relaxation contribution and, with the aid of a model for tumbling proteins [P.-O. Westlund, Phys. Chem. Chem. Phys, 12, 3136 (2010)], it is shown that the QP effect is absent in water-proton T 1-NMRD profiles for slow tumbling proteins with τR < 1 µs, τI.

Place, publisher, year, edition, pages
2012. Vol. 110, no 18, 2251-2255 p.
Keyword [en]
H–N cross-relaxation, quadrupole peak effect, stochastic Liouville equation, water T 1-NMRD profiles, slow tumbling proteins
National Category
Chemical Sciences
URN: urn:nbn:se:umu:diva-54602DOI: 10.1080/00268976.2012.674566OAI: diva2:524369

Available online: 20 Mar 2012

Available from: 2012-05-02 Created: 2012-05-02 Last updated: 2012-11-07Bibliographically approved

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