title: X-ray reflectivity measurements of liquid/solid interfaces under high hydrostatic pressure conditions.
abstract: A high-pressure cell for in situ X-ray reflectivity measurements of liquid/solid interfaces at hydrostatic pressures up to 500 MPa (5 kbar), a pressure regime that is particularly important for the study of protein unfolding, is presented. The original set-up of this hydrostatic high-pressure cell is discussed and its unique properties are demonstrated by the investigation of pressure-induced adsorption of the protein lysozyme onto hydrophobic silicon wafers. The presented results emphasize the enormous potential of X-ray reflectivity studies under high hydrostatic pressure conditions for the in situ investigation of adsorption phenomena in biological systems.
authors.affiliation: Fakultät Physik/DELTA, TU Dortmund, 44221 Dortmund, Germany.
authors.forename: Florian J
authors.initials: FJ
authors.lastname: Wirkert
authors.affiliation: Fakultät Physik/DELTA, TU Dortmund, 44221 Dortmund, Germany.
authors.forename: Michael
authors.initials: M
authors.lastname: Paulus
authors.affiliation: Fakultät Physik/DELTA, TU Dortmund, 44221 Dortmund, Germany.
authors.forename: Julia
authors.initials: J
authors.lastname: Nase
authors.affiliation: Fakultät Physik/DELTA, TU Dortmund, 44221 Dortmund, Germany.
authors.forename: Johannes
authors.initials: J
authors.lastname: Möller
authors.affiliation: Fakultät Physik/DELTA, TU Dortmund, 44221 Dortmund, Germany.
authors.forename: Simon
authors.initials: S
authors.lastname: Kujawski
authors.affiliation: Fakultät Physik/DELTA, TU Dortmund, 44221 Dortmund, Germany.
authors.forename: Christian
authors.initials: C
authors.lastname: Sternemann
authors.affiliation: Fakultät Physik/DELTA, TU Dortmund, 44221 Dortmund, Germany.
authors.forename: Metin
authors.initials: M
authors.lastname: Tolan
mesh_terms: D006874:Hydrostatic Pressure; D009113:Muramidase / Q000737:chemistry; D013499:Surface Properties; D014965:X-Rays
chemical_list: D009113:Muramidase
keywords: X-ray reflectivity; high hydrostatic pressure; protein adsorption