Document Type

Thesis

Date of Award

5-31-1987

Degree Name

Master of Science in Chemical Engineering - (M.S.)

Department

Chemical Engineering, Chemistry and Environmental Science

First Advisor

Carol A. Venanzi

Second Advisor

Tamara M. Gund

Third Advisor

Dana E. Knox

Abstract

Molecular mechanics calculations were used to investigate the structural flexibility of the norbornane mimic which is a model of an acyl-alpha-chymotrypsin intermediate. The Amber molecular mechanics force field was used to perform the conformational analysis.

Comparison of the optimized conformations of different energy has shown the relative structural rigidity of this molecule. Structural superposition of the minimized mimic to the native conformation of chymotrypsin shows that the mimic has a very similar spatial arrangement of its functional groups compared to the catalytic triad of the real enzyme.

Molecular electrostatic potential maps calculated in planes parallel to the average plane containing the catalytic triad indicate that the mimic presents an electrostatic pattern similar to that of chymotrypsin in the region of the carboxylate fragment.

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