When cells are subjected to stress, such as drying, globular proteins are observed to unfold and irreversibly aggregate. Certain intrinsically disordered proteins (IDPs) do not do this and they also protect globular proteins from aggregation. We wish to understand how the proteins interact and the mechanism by which the IDP's stop further aggregation. We will examine the aggregation of two model proteins, citrate synthase and AavLEA1, an intrinsically disordered protein. Preliminary studies have indicated that there is no intraction between the two proteins, until the system is subjected to drying. The observed interaction seems to be consistent with a layering and maybe a steric stabilisation of the globular protein by the IDP. We wish to investigate this. We will selectively deuterate one of the proteins and so separately examine both components in the flocs.