Osmotic pressure effects on collagen mimetic peptides Collagen is the most abundant protein in mammals. In many tissues collagen molecules assemble to form a hierarchical structure. In the smallest supramolecular unit named fibril each molecule is displaced in the axial direction with respect to its neighbors. This staggering creates a periodic gap and overlap regions where the gap regions exhibit 20% less density. These fibril forming collagens play an essential role in the strength of connective tissues. Despite much effort directed at understanding collagen function and regulation the influence of the chemical environment on the local structural and mechanical properties remains poorly understood. Recent studies aimed at elucidating the effect of osmotic pressure showed that collagen contracts upon water removal. This observation highlights the importance of water for the stabilization and mechanics of the collagen molecule. Using collagen mimetic peptides (CMPs) which fold into triple helical structures reminiscent of natural collagen the primary goal of this work was to investigate the effect of the osmotic pressure on specific collagen mimetic sequences. ...