Amyloid fibrils are filamentous structures with remarkably similar morphologies formed by a variety of polypeptides with remarkably dissimilar amino acid sequences. We are using novel nuclear magnetic resonance (NMR) techniques to investigate the molecular structures of amyloid fibrils, especially amyloid fibrils that deposit in the brains of Alzheimer’s disease patients. Physics plays two roles in this highly interdisciplinary work: (1) fundamental physical issues, such as the nature of interactions that stabilize amyloid fibrils, are unresolved and motivate our measurements; (2) the NMR techniques themselves involve interesting physical principles and phenomena. Our most recent progress will be described, with an emphasis on the physical science aspects.