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Small-angle neutron scattering (SANS) is uniquely suited to the study of biological systems in solution in the size range from 10 Å to 1000 Å. In the case of protein aggregates, SANS is sensitive to structures at all of these length scales, from the total aggregate size down to the monomer size. Thus, it is possible to observe scattering over a wide range of length scales and to follow the change in morphology of a protein system as it assembles into aggregates. In addition, neutrons are especially sensitive to the light elements, such as H, C, N, and O, which are of importance in biological systems. Finally, neutrons are highly penetrating yet nondestructive, so proteins can be studied in solution under conditions that closely mimic their native environment. The radius of gyration and molecular weight of proteins and protein aggregates in solution can be extracted directly from SANS data.With more detailed data analysis involving comparison to model structures, information about overall particle shape and particle size distribution, as well as interparticle interactions, can be obtained. Examples of SANS experiments that have contributed to a better understanding of the mechanism of different types of protein aggregation in solution are presented. [ABSTRACT FROM AUTHOR]