Göhring, HolgerHolgerGöhringPaulus, MichaelMichaelPaulusSalmen, PaulPaulSalmenWirkert, FlorianFlorianWirkertKruse, TheresaTheresaKruseDegen, PatrickPatrickDegenStuhr, SusanSusanStuhrRehage, HeinzHeinzRehageTolan, MetinMetinTolan2021-01-272021-01-272015-06-17https://resolver.sub.uni-goettingen.de/purl?gro-2/79473A study of lysozyme adsorption below a behenic acid membrane and at the solid-liquid interface between aqueous lysozyme solution and a silicon wafer in the presence of sodium chloride is presented. The salt concentration was varied between 1 mmol L(-1) and 1000 mmol L(-1). X-ray reflectivity data show a clear dependence of the protein adsorption on the salt concentration. Increasing salt concentrations result in a decreased protein adsorption at the interface until a complete suppression at high concentrations is reached. This effect can be attributed to a reduced attractive electrostatic interaction between the positively charged proteins and negatively charged surfaces by charge screening. The measurements at the solid-liquid interfaces show a transition from unoriented order of lysozyme in the adsorbed film to an oriented order with the short protein axis perpendicular to the solid-liquid interface with rising salt concentration.enjournal_article10.1088/0953-8984/27/23/23510325992483