The study of macromolecular interactions in three systems: The basic-helix-loop-helix DNA binding motif, dissociative inhibition of an enzyme, and intramolecular disulfide bond formation reactions
Abstract
Three systems were studied that involved interactions between macromolecular structures. The basic-helix-loop-helix region of the Immunoglobulin Enhancer Binding Protein-E47 was studied to develop a methodology such that the basic-helix-loop-helix of Tal could be studied. Results indicated that the basic-helix-loop-helix of Tal homodimerized but these complexes did not bind a DNA probe containing three E box sequences. A fusion protein was synthesized to investigate the effect of the helix-loop-helix region of Tal on its DNA binding activities. That this protein did not bind the DNA probe indicated that the Tal homodimers may have another sequence specificity. The second system involved the study of agents designed to inhibit the protease of the Human Immunodeficiency Virus by dissociative inhibition. Modifications were made to the inhibitor to understand the interactions with the protease, and a fluorescence assay was developed to show that the agents were interfering with dimerization. The third system involved the development of two new reagents for intramolecular disulfide bond formation in peptides, cyanogen iodide and dimethyl(methylthio)sulfonium tetrafluoroborate.
Degree
Ph.D.
Advisors
Chmielewski, Purdue University.
Subject Area
Organic chemistry|Biochemistry
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