Work is proposed on the following problems: (1) Self-association of insulin (in particular the dimerization), will be studied with native and specifically-modified protein, using concentration difference spectra. (2) Dissociation of hemoglobin will be studied also using specifically-modified protein, and an attempt will be made to develop a tracer technique for measuring dissociation at low protein concentration. (3) Several aspects of lysozyme chemistry are to be examined including interaction with saccharides and other small ligands, tryptophan properties, and self-association. Enthalpy measurements (microcalorimetry) are emphasized. (4) Computation of changes in group environments (exposure) that follow protein folding, for correlation of crystal structure with chemistry, will be continued.