Funds are requested for a circular dichroism (CD) spectropolarimeter. There is no CD instrument at UNC-CH. Most of the experiments proposed involve examination of protein secondary structure by observation of Cotton effects in the ultraviolet. The proteins and peptides to be studied include: (1) native and denatured variants of Saccharomyces cerevisiae iso-1-cytochrome c, (2) coagulation proteins containing gamma- carboxy glutamic acid in the presence and absence of divalent metal ions and/or negatively-charged phospolipids, (3) ribosomes and their co-factors, (4) regulatory proteins and peptides of the coagulation system in the presence and absence glycosaminglycans, (5) non-genetic proteins synthesized to have special structural and chemical properties and (6) ultrathin polypeptide-silica structures. Linear dichroism will also be examined for the ultrathin polypeptide-silica structures. Ultraviolet CD spectra will be used to assign absolute configurations of transition metal complexes of importance for synthesis of highly-pure molecules for biotechnology. CD in the visible region will be examined to determine the absolute configuration of chiral organometallic complexes used for enantioselective organic reactions. CD in the visible and near infrared regions as well as magnetic CD will be examined to determine the heme environment of cytochrome c variants and for investigation of the active site geometry of Co(II)-substituted cytidine deaminase.
