The study used NMR to look at how the small peptide thymosin‑beta‑4 fragment and a piece of the stabilin protein behave in water and how they bind together. It found that the complex they form is quite flexible and has a lot of disordered parts, with about 40% of the peptide’s binding sites involved in the interaction.

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-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.