The formation of a protein corona occurs on all surfaces exposed to biological systems and understanding of how this corona forms is vital for many aspects of medicine and for assessing potential dangers from nanoparticle exposure. The most fundamental process underlying exchange of different proteins in a mixture with the surface is self-exchange of any given protein with the surface. This can only be measured by neutron reflectometry using exchange of protonated and deuterated proteins. We have recently been able to test out the ILL deuteration facilities standard "protein for physicists", MPB, and we have found that it has surface properties fairly similar to those of HSA, one of the key proteins in protein corona formation. We therefore propose to study the self-exchange kinetics of MPB with three different solid/liquid surfaces, hydrophilic, hydrophobic and their intermediate