Circular Dichroism Spectrometer

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A group of researchers at the University of Louisville requests funding for half of the cost of a circular dichroism spectrometer, which will be used for assessing peptide and protein secondary structure in solution, for investigating changes in protein conformation induced by alterations in temperature, solvent, pH, or ligand binding, and for conformational analysis of synthetic polypeptides and recombinant proteins. The specific projects proposed include application of circular dichroism to the following systems: (1) purified, soluble cytochrome P-450 isozymes, and the membrane anchoring peptide of NADPH-cytochrome P-450 reductase, (2) cytoplasmic and microsomal enzymes involved in the metabolism of foreign compounds, (3) recombinant human fibroblast procollagenase and collagenase, (4) native RNA processing enzymes and recombinant enzymes altered by site-directed mutagenesis, (5) mitochondrial targeting signal peptides, (6) Ca++ -induced conformational changes in chromogranin A, and (7) synthetic peptides containing amide bond replacements (pseudopeptides).