Protein aggregation and gel formation studied with scattering methods and computer simulations

We review recent scattering experiments on the reversible and irreversible aggregation and gelation of globular proteins. Globular proteins are compact with a well-defined structure in the native state, but are not perfect spheres and the details of the interaction between proteins may be intricate involving for instance specific binding sites. Nevertheless, it turns out that often the structure of globular protein aggregates and gels can be understood by treating them as spherical colloids with relatively simple interaction potentials. Computer simulations of interacting hard spheres give detailed structural information that can be used to understand some aspects of protein aggregation and gel formation. (c) 2007 Elsevier Ltd. All rights reserved.