Hydration shells of normal proteins display both structured and bulk- like waters. Isomers with considerable bulk-like hydration tend to aggregate. In my talk, I will present both theoretical and experimental data showing that different morphological states of aggregated isomers differ by hydration distribution profiles and water magnetic resonance (MR) signals. The results help explain the MR contrast patterns of amyloids, a subject of long controversy, and suggest a new approach for identifying unusual protein aggregation related to disease. As an example, I will present MRI data and cell toxicity measurements revealing the relationship between the structural conformations of several amyloidogenic peptides and the mechanisms of cellular dysfunction.