This laboratory is interested in the relationship among protein sequence, structure and the mechanisms of protein folding and enzymic reactions. (i) Secondary Structure of Amyloid Proteins. g-factor analysis of the CD spectra of amyloid proteins and polypeptides indicate the presence of two types of structure. Amyloid forms of ovalbumin, apomyoglobin, transthyretin and Ure2p contain 35-55% of beta sheet, whose CD spectrum is like that found in most globular proteins. The more intense spectra of beta-2-microglobulin, insulin, Abeta(1-40) peptide and various homopolypetides, in amyloid films are consistent with the presence of 50-80% of beta helix like structure(ii)hormone receptors (with Dr. Jane Cheng, NCI) Mutations in the hormone binding domain of these proteins change their affinity for hormone and their activity as activators. (vii) Effect of molecular crowding and confinement on protein stability (with YiSheng Ni and Allen Minton, NIDDK).