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Water-mediated protein-protein interactions at high pressures are controlled by a deep-sea osmolyte

DOI: 10.1103/PhysRevLett.121.038101 DOI Help

Authors: Karin Julius (TU Dortmund University) , Jonathan Weine (TU Dortmund University) , Melanie Berghaus (TU Dortmund University) , Nico König (TU Dortmund University) , Mimi Gao (TU Dortmund University) , Jan Latarius (TU Dortmund University) , Michael Paulus (TU Dortmund University) , Martin A. Schroer (European Molecular Biology Laboratory (EMBL) Hamburg c/o DESY) , Metin Tolan (TU Dortmund University) , Roland Winter (TU Dortmund University)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Physical Review Letters , VOL 121

State: Published (Approved)
Published: July 2018
Diamond Proposal Number(s): 14949

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.

Journal Keywords: Biomolecular interactions; Biomolecular self-assemblyl; Osmosis; Proteins; X-ray scattering

Subject Areas: Chemistry, Biology and Bio-materials


Instruments: I22-Small angle scattering & Diffraction

Other Facilities: ESRF; DELTA; SOLEIL