Molecular Motions and Interactions in Aqueous Solutions of Thymosin-beta4 , Stabilin C-Terminal Domain (CTD) and Their 1:1 Complex Studied by (1) H NMR Spectroscopy

Bokor, Mónika Zsuzsanna and Tantos, Ágnes and Mészáros, Attila and Jenei, Bence and Haminda, Réka and Tompa, Péter and Tompa, Kálmán (2018) Molecular Motions and Interactions in Aqueous Solutions of Thymosin-beta4 , Stabilin C-Terminal Domain (CTD) and Their 1:1 Complex Studied by (1) H NMR Spectroscopy. CHEMPHYSCHEM: A EUROPEAN JOURNAL OF CHEMICAL PHYSICS AND PHYSICAL CHEMISTRY, 19 (7). pp. 848-856. ISSN 1439-4235

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Official URL: https://doi.org/10.1002/cphc.201701187

Abstract

Wide-line (1) H NMR measurements were extended and all results were reinterpreted in a new thermodynamics-based approach to study aqueous solutions of thymosin-beta4 (Tbeta4 ), stabilin C-terminal domain (CTD) and their 1:1 complex. The energy distributions of the potential barriers, which control motion of protein-bound water molecules, were determined. Heterogeneous and homogeneous regions were found at the protein-water interface. The measure of heterogeneity gives a quantitative value for the portion of disordered parts in the protein. Ordered structural elements were found extending up to 20 % of the whole proteins. About 40 % of the binding sites of free Tbeta4 become involved in bonds holding the complex together. The complex has the most heterogeneous solvent accessible surface (SAS) in terms of protein-water interactions. The complex is more disordered than Tbeta4 or stabilin CTD. The greater SAS area of the complex is interpreted as a clear sign of its open structure.

Item Type:	Article
Additional Information:	Megjegyzés-27441793 N1 Funding details: FWO, Fonds Wetenschappelijk Onderzoek N1 Funding details: G.0029.12, KRCF, Korea Research Council of Fundamental Science and Technology N1 Funding details: ANN-11056 N1 Funding text: The authors wish to thank to the National Research, Development and Innovation Office (Hungary) for grant ANN-11056. They are thankful for the Korean-Hungarian Joint Laboratory grant from Korea Research Council of Fundamental Science and Technology. P. T. also acknowledges the Odysseus grant G.0029.12 from Research Foundation Flanders. Megjegyzés-27445372 N1 Funding details: FWO, Fonds Wetenschappelijk Onderzoek N1 Funding details: G.0029.12, KRCF, Korea Research Council of Fundamental Science and Technology N1 Funding details: ANN-11056 N1 Funding text: The authors wish to thank to the National Research, Development and Innovation Office (Hungary) for grant ANN-11056. They are thankful for the Korean-Hungarian Joint Laboratory grant from Korea Research Council of Fundamental Science and Technology. P. T. also acknowledges the Odysseus grant G.0029.12 from Research Foundation Flanders. Megjegyzés-27448539 N1 Funding details: FWO, Fonds Wetenschappelijk Onderzoek N1 Funding details: G.0029.12, KRCF, Korea Research Council of Fundamental Science and Technology N1 Funding details: ANN-11056 N1 Funding text: The authors wish to thank to the National Research, Development and Innovation Office (Hungary) for grant ANN-11056. They are thankful for the Korean-Hungarian Joint Laboratory grant from Korea Research Council of Fundamental Science and Technology. P. T. also acknowledges the Odysseus grant G.0029.12 from Research Foundation Flanders. Megjegyzés-27448802 N1 Funding details: FWO, Fonds Wetenschappelijk Onderzoek N1 Funding details: G.0029.12, KRCF, Korea Research Council of Fundamental Science and Technology N1 Funding details: ANN-11056 N1 Funding text: The authors wish to thank to the National Research, Development and Innovation Office (Hungary) for grant ANN-11056. They are thankful for the Korean-Hungarian Joint Laboratory grant from Korea Research Council of Fundamental Science and Technology. P. T. also acknowledges the Odysseus grant G.0029.12 from Research Foundation Flanders. Megjegyzés-27448891 N1 Funding details: FWO, Fonds Wetenschappelijk Onderzoek N1 Funding details: G.0029.12, KRCF, Korea Research Council of Fundamental Science and Technology N1 Funding details: ANN-11056 N1 Funding text: The authors wish to thank to the National Research, Development and Innovation Office (Hungary) for grant ANN-11056. They are thankful for the Korean-Hungarian Joint Laboratory grant from Korea Research Council of Fundamental Science and Technology. P. T. also acknowledges the Odysseus grant G.0029.12 from Research Foundation Flanders. Export Date: 27 December 2018 CODEN: CPCHF
Uncontrolled Keywords:	BINDING; CONFORMATION; PROTEIN INTERACTIONS; DYNAMICS; WATER; HYDRATION; NUCLEAR-MAGNETIC-RESONANCE; NMR spectroscopy; PROTEIN-PROTEIN INTERACTIONS; PROTEIN COMPLEXES; PROMOTION; POTENTIAL BARRIER; FUZZY COMPLEXES; BETA-4;
Subjects:	Q Science / természettudomány > QC Physics / fizika > QC06 Physics of condensed matter / szilárdtestfizika Q Science / természettudomány > QH Natural history / természetrajz > QH301 Biology / biológia > QH3011 Biochemistry / biokémia Q Science / természettudomány > QH Natural history / természetrajz > QH301 Biology / biológia > QH3015 Molecular biology / molekuláris biológia
SWORD Depositor:	MTMT SWORD
Depositing User:	MTMT SWORD
Date Deposited:	07 Mar 2019 07:49
Last Modified:	07 Mar 2019 07:49
URI:	http://real.mtak.hu/id/eprint/91849

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