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Published on: January 20, 2022
Water-Mediated Protein-Protein Interactions at High Pressures are Controlled by a Deep-Sea Osmolyte
Karin Julius1, Jonathan Weine1, Melanie Berghaus2
1Faculty of Physics/DELTA, TU Dortmund University, 44221 Dortmund, Germany.
Abstract:
The influence of natural cosolvent mixtures on the pressure-dependent structure and protein-protein interaction potential of dense protein solutions is studied and analyzed using small-angle X-ray scattering in combination with a liquid-state theoretical approach. The deep-sea osmolyte trimethylamine-N-oxide is shown to play a crucial and singular role in its ability to not only guarantee sustainability of the native protein's folded state under harsh environmental conditions, but it also controls water-mediated intermolecular interactions at high pressure, thereby preventing contact formation and hence aggregation of proteins.
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