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Retracted: Molecular Motions and Interactions in Aqueous Solutions of Thymosin‐β 4 , Stabilin C‐Terminal Domain (CTD) and Their 1:1 Complex Studied by 1 H NMR Spectroscopy
Author(s) -
Bokor Mónika,
Tantos Ágnes,
Mészáros Attila,
Jenei Bence,
Haminda Réka,
Tompa Péter,
Tompa Kálmán
Publication year - 2018
Publication title -
chemphyschem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.016
H-Index - 140
eISSN - 1439-7641
pISSN - 1439-4235
DOI - 10.1002/cphc.201701187
Subject(s) - ctd , aqueous solution , chemistry , nuclear magnetic resonance spectroscopy , crystallography , chemical physics , molecular dynamics , molecule , domain (mathematical analysis) , spectroscopy , solvent , analytical chemistry (journal) , computational chemistry , stereochemistry , physics , organic chemistry , quantum mechanics , geology , mathematical analysis , oceanography , mathematics
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‐β 4 (Tβ 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 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 Tβ 4 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 Tβ 4 or stabilin CTD. The greater SAS area of the complex is interpreted as a clear sign of its open structure.