Molecular motions and interactions in aqueous solutions of thymosin-ß4, stabilin CTD and their 1:1 complex, studied by 1H-NMR spectroscopy.
Related Articles Molecular motions and interactions in aqueous solutions of thymosin-ß4, stabilin CTD and their 1:1 complex, studied by 1H-NMR spectroscopy.
Chemphyschem. 2017 Dec 23;:
Authors: Bokor M, Tantos Á, Mészáros A, Jenei B, Haminda R, Tompa P, Tompa K
Abstract
Wide-line 1H NMR measurements were extended and all results were reinterpreted in a thermodynamics based new approach on aqueous solutions of thymosin-?4 (T?4), 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 homo-geneous regions were found in the protein-water interface. The measure of heterogeneity give 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 T?4 get involved in bonds holding the complex together. The complex has the most heterogeneous solvent accessible surface (SAS) in terms of protein-water interactions. According to the used terminology, the complex is more disordered than T?4 or stabilin CTD. The greater SAS area of the complex is interpreted as a clear sign of its open structure.
PMID: 29274195 [PubMed - as supplied by publisher]
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