The main effort in this project will be the evaluation and interpretation of the thermodynamics of various processes of biochemical interest. in most cases the primary method of investigation will be isothermal titration calorimetry. other observational techniques will be employed as appropriate, including differential scanning microcalorimetry, fluorescence emission and CED and UV spectrometry. A large fraction of the research will be carried out in collaboration with individuals in other laboratories. The phenomena to be studied will include the following: (1) The binding of glycopeptides to concanavalin A; (2) The interaction of modified S-Peptides with S-protein to form modified ribonuclease S; (3) The binding of substrate analogs and inhibitors to wild type and mutant forms of ribonuclease T1, staphylococcal nuclease, and T4 lysozyme; (4) The interaction between mutated forms of Streptomyces subtilisin inhibitor and subtilisin and other proteases; (5) The binding of modified corepressors to E. coli tryptophan aporepressor; (6) The effect of glycosylation on the thermal stability of proteins such as staphylococcal nuclease and takamylase; and the binding of cyclosporin by cyclophyllin.
