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      Dynamics of Solid Proteins by Means of Nuclear Magnetic Resonance Relaxometry

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          Abstract

          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.

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          Structural and immunologic characterization of bovine, horse, and rabbit serum albumins.

          Serum albumin (SA) is the most abundant plasma protein in mammals. SA is a multifunctional protein with extraordinary ligand binding capacity, making it a transporter molecule for a diverse range of metabolites, drugs, nutrients, metals and other molecules. Due to its ligand binding properties, albumins have wide clinical, pharmaceutical, and biochemical applications. Albumins are also allergenic, and exhibit a high degree of cross-reactivity due to significant sequence and structure similarity of SAs from different organisms. Here we present crystal structures of albumins from cattle (BSA), horse (ESA) and rabbit (RSA) sera. The structural data are correlated with the results of immunological studies of SAs. We also analyze the conservation or divergence of structures and sequences of SAs in the context of their potential allergenicity and cross-reactivity. In addition, we identified a previously uncharacterized ligand binding site in the structure of RSA, and calcium binding sites in the structure of BSA, which is the first serum albumin structure to contain metal ions. Copyright © 2012 Elsevier Ltd. All rights reserved.
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            Dynamic effects of pair correlation functions on spin relaxation by translational diffusion in liquids

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              Field-cycling NMR relaxometry

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                Author and article information

                Journal
                Biomolecules
                Biomolecules
                biomolecules
                Biomolecules
                MDPI
                2218-273X
                25 October 2019
                November 2019
                : 9
                : 11
                Affiliations
                [1 ]Faculty of Mathematics and Computer Science, University of Warmia and Mazury in Olsztyn, Słoneczna 54, 10-710 Olsztyn, Poland; elzbieta.masiewicz@ 123456matman.uwm.edu.pl (E.M.); a.borkowska@ 123456uwm.edu.pl (A.M.B.); pawel.rochowski@ 123456gmail.com (P.R.)
                [2 ]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; pascal-h.fries@ 123456cea.fr
                [3 ]Bio-Medical Physics, School of Medicine, Medical Sciences & Nutrition, University of Aberdeen, Foresterhill, Aberdeen, Scotland AB25 2ZD, UK; l.broche@ 123456abdn.ac.uk (L.M.B.); d.lurie@ 123456abdn.ac.uk (D.J.L.)
                Author notes
                [* ]Correspondence: danuta.kruk@ 123456matman.uwm.edu.pl ; Tel.: +48-89-524-6011
                [†]

                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; p.rochowski@ 123456ug.edu.pl .

                Article
                biomolecules-09-00652
                10.3390/biom9110652
                6920843
                31731514
                8bfdc041-cc32-499a-95e3-973af51e5f1c
                © 2019 by the authors.

                Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license ( http://creativecommons.org/licenses/by/4.0/).

                Categories
                Article

                proteins,relaxation,dynamics,nmr relaxometry,quadrupole relaxation enhancement,solids

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