Connor Galvin

Date of Award

2019

Document Type

Thesis

Degree Name

Bachelors

Department

Natural Sciences

First Advisor

Shipman, Steven

Area of Concentration

Chemistry

Abstract

Previous comparative analyses of homologous thermophilic and mesophilic proteins have consistently shown increased numbers of charged amino acids and ion pairing interactions within the thermophilic structures. While the electrostatic energies of thermophilic proteins have been shown to be more favorable than those of mesophiles, the physical determinants for this enhanced stabilizing effect have remained unclear. In order to address this problem, we compared ten features of the charge distributions in high quality crystal structures of 104 thermophilic and 118 mesophilic subunits from 90 different protein families. Substantial differences were found for eight of the features investigated, including several that have not been previously reported. The observed preferences of the thermophilic charge distributions may be useful to protein engineering efforts aimed at redesigning the charge distributions in mesostable proteins for increased stability.

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