The structure of large biomolecules is in many cases the key for understanding their function. For decades the molecular structure of biomolecules has been revealed with the help of X-ray scattering at crystals. These first had to be produced in a laborious process. With the advent of free electron lasers, light sources became brilliant enough to enable X ray scattering of single proteins, and offer the potential to circumvent the need to produce protein crystals. During such single particle X-ray scattering measurements, the proteins’ orientation is undefined and the analysis of the data requires us to find the orientation for each single shot in a computationally very expensive process. Some of the computational cost could be alleviated if the sample molecules could be oriented before the measurement and massively improve the capabilities of the technique. One way to potentially achieve this goal is to use an aqueous interface as a tool to force biomolecules into a known orientation. To this end, we developed a hybrid simulation approach employing a combination of non-local thermodynamic equilibrium and extensive classical molecular dynamics simulations. The simulations will focus on the role of inorganic ions and pH as tools to control the orientation of the large peptides and proteins at a liquid surface.