Date of Defense

Winter 1989

Department

Biological Sciences

First Advisor

Howard Einspahr, Upjohn Company

Second Advisor

Jochanan Stenesh, Chemistry

Third Advisor

Leonard Ginsberg, Biological Sciences

Abstract

Protein crystallography uses X-ray diffraction techniques to determine the three-dimensional structures of proteins. Proteins are molecules with complex structure, and the diversity of the biological functions they express is determined by, and is dependent upon, the diversity of the tertiary structures they adopt, and upon the abilities of these structures to respond to other molecules by changes in shape and chemistry. At the present time, protein crystallography is the most widely applicable method of acquiring significant new structural data, and the detail it provides is unequalled by any other technique. Together with biochemical and chemical studies, the structural information acquired provides information upon which proposals concerning the molecular basis of biological activity can be based. The goal of the project described in this thesis is to optimize methods for crystallizing a copperhead phospholipase A2 enzyme both in its free state and complexed with an inhibitor. This thesis presents a brief description of the biological properties of phospholipases A2 and provides a synopsis of a variety of methods used for protein crystallization. A materials and methods section describes the techniques that were employed, and the actual experiments carried out for this project. The crystallization results are presented and discussed in the final sections.

Access Setting

Honors Thesis-Campus Only

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