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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
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