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Open AccessArticle

Dynamics of Solid Proteins by Means of Nuclear Magnetic Resonance Relaxometry

Faculty of Mathematics and Computer Science, University of Warmia and Mazury in Olsztyn, Słoneczna 54, 10-710 Olsztyn, Poland
Laboratoire de Reconnaissance Ionique et Chimie de Coordination, Service de Chimie Inorganique et Biologique (UMR E-3 CEA/UJF), CEA-Grenoble, INAC, 17 rue des Martyrs, CEDEX 09, 38054 Grenoble, France
Bio-Medical Physics, School of Medicine, Medical Sciences & Nutrition, University of Aberdeen, Foresterhill, Aberdeen, Scotland AB25 2ZD, UK
Author to whom correspondence should be addressed.
Current affiliation of Pawel Rochowski: Institute of Experimental Physics, Faculty of Mathematics, Physics and Informatics, University of Gdańsk, Wita Stwosza 57, 80-308 Gdańsk, Poland
Biomolecules 2019, 9(11), 652;
Received: 27 September 2019 / Revised: 16 October 2019 / Accepted: 19 October 2019 / Published: 25 October 2019
(This article belongs to the Section Biomacromolecules)
1H Nuclear magnetic resonance (NMR) relaxometry was exploited to investigate the dynamics of solid proteins. The relaxation experiments were performed at 37 °C over a broad frequency range, from approximately 10 kHz to 40 MHz. Two relaxation contributions to the overall 1H spin–lattice relaxation were revealed; they were associated with 1H–1H and 1H–14N magnetic dipole–dipole interactions, respectively. The 1H–1H relaxation contribution was interpreted in terms of three dynamical processes occurring on timescales of 10−6 s, 10−7 s, and 10−8 s, respectively. The 1H–14N relaxation contribution shows quadrupole relaxation enhancement effects. A thorough analysis of the data was performed revealing similarities in the protein dynamics, despite their different structures. Among several parameters characterizing the protein dynamics and structure (e.g., electric field gradient tensor at the position of 14N nuclei), the orientation of the 1H–14N dipole–dipole axis, with respect to the principal axis system of the electric field gradient, was determined, showing that, for lysozyme, it was considerably different than for the other proteins. Moreover, the validity range of a closed form expression describing the 1H–14N relaxation contribution was determined by a comparison with a general approach based on the stochastic Liouville equation. View Full-Text
Keywords: proteins; relaxation; dynamics; NMR relaxometry; quadrupole relaxation enhancement; solids proteins; relaxation; dynamics; NMR relaxometry; quadrupole relaxation enhancement; solids
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Kruk, D.; Masiewicz, E.; Borkowska, A.M.; Rochowski, P.; Fries, P.H.; Broche, L.M.; Lurie, D.J. Dynamics of Solid Proteins by Means of Nuclear Magnetic Resonance Relaxometry. Biomolecules 2019, 9, 652.

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