title: Nonlinear pressure dependence of the interaction potential of dense protein solutions.
abstract: The influence of pressure on the structure and protein-protein interaction potential of dense protein solutions was studied and analyzed using small-angle x-ray scattering in combination with a liquid state theoretical approach. The structural as well as the interaction parameters of dense lysozyme solutions are affected by pressure in a nonlinear way. The structural properties of water lead to a modification of the protein-protein interactions below 4 kbar, which might have significant consequences for the stability of proteins in extreme natural environments.
authors.affiliation: Faculty of Physics/DELTA, TU Dortmund, Maria-Goeppert-Mayer-Str. 2, 44227 Dortmund, Germany.
authors.forename: Martin A
authors.initials: MA
authors.lastname: Schroer
authors.forename: Jonas
authors.initials: J
authors.lastname: Markgraf
authors.forename: D C Florian
authors.initials: DC
authors.lastname: Wieland
authors.forename: Christoph J
authors.initials: CJ
authors.lastname: Sahle
authors.forename: Johannes
authors.initials: J
authors.lastname: Möller
authors.forename: Michael
authors.initials: M
authors.lastname: Paulus
authors.forename: Metin
authors.initials: M
authors.lastname: Tolan
authors.forename: Roland
authors.initials: R
authors.lastname: Winter
mesh_terms: D006863:Hydrogen-Ion Concentration; D008956:Models, Chemical; D009113:Muramidase / Q000737:chemistry* / Q000378:metabolism; D017711:Nonlinear Dynamics; D011312:Pressure; D017510:Protein Folding; D017433:Protein Structure, Secondary; D012542:Scattering, Radiation; D012996:Solutions / Q000737:chemistry*; D014965:X-Rays
chemical_list: D012996:Solutions; D009113:Muramidase