Molecular Motions and Interactions in Aqueous Solutions of Thymosin-β4, Stabilin C-Terminal Domain (CTD) and Their 1: 1 Complex Studied by 1H NMR Spectroscopy

M. Bokor, Ágnes Tantos, Attila Mészáros, Bence Jenei, Réka Haminda, Péter Tompa, K. Tompa

Research output: Contribution to journalArticle

Abstract

Wide-line 1H NMR measurements were extended and all results were reinterpreted in a new thermodynamics-based approach to study aqueous solutions of thymosin-β4 (Tβ4), 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 Tβ4 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 Tβ4 or stabilin CTD. The greater SAS area of the complex is interpreted as a clear sign of its open structure.

Original languageEnglish
Pages (from-to)848-856
Number of pages9
JournalChemPhysChem
Volume19
Issue number7
DOIs
Publication statusPublished - Apr 5 2018

Fingerprint

Thymosin
Nuclear magnetic resonance spectroscopy
aqueous solutions
proteins
nuclear magnetic resonance
spectroscopy
Proteins
interactions
Motion control
energy distribution
Binding Sites
Nuclear magnetic resonance
Thermodynamics
thermodynamics
Molecules
Water
water
molecules

Keywords

  • hydration
  • NMR spectroscopy
  • potential barrier
  • protein complexes
  • protein–protein interactions

ASJC Scopus subject areas

  • Atomic and Molecular Physics, and Optics
  • Physical and Theoretical Chemistry

Cite this

Molecular Motions and Interactions in Aqueous Solutions of Thymosin-β4, Stabilin C-Terminal Domain (CTD) and Their 1 : 1 Complex Studied by 1H NMR Spectroscopy. / Bokor, M.; Tantos, Ágnes; Mészáros, Attila; Jenei, Bence; Haminda, Réka; Tompa, Péter; Tompa, K.

In: ChemPhysChem, Vol. 19, No. 7, 05.04.2018, p. 848-856.

Research output: Contribution to journalArticle

Bokor, M. ; Tantos, Ágnes ; Mészáros, Attila ; Jenei, Bence ; Haminda, Réka ; Tompa, Péter ; Tompa, K. / Molecular Motions and Interactions in Aqueous Solutions of Thymosin-β4, Stabilin C-Terminal Domain (CTD) and Their 1 : 1 Complex Studied by 1H NMR Spectroscopy. In: ChemPhysChem. 2018 ; Vol. 19, No. 7. pp. 848-856.
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