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Date Permissions Signed

7-27-2015

Date of Award

Summer 2015

Document Type

Masters Thesis

Degree Name

Master of Science (MS)

Department

Chemistry

First Advisor

Antos, John M.

Second Advisor

Murphy, Amanda R.

Third Advisor

Anthony-Cahill, Spencer J.

Abstract

The use of enzymes for protein modification chemistry has gained traction in recent years due to the remarkable site-selectivity that enzymes afford. Among enzymes reported for this purpose, sortase A from Staphylococcus aureus (SrtAStaph) has garnered significant attention because of its selectivity, and its ability to install a wide range of non-natural modifications. In addition to SrtAStaph, it is now appreciated that sortase homologs exist in many bacterial strains, each with the potential to serve as a new catalyst for protein engineering. However, the majority of these enzymes has not been studied biochemically, and in order to utilize these enzymes for protein modification it is critical that the activity and specificity of each enzyme be verified experimentally. This includes determination of optimal substrate sequences and amine nucleophile preferences. Here we present progress toward characterizing the in vitro substrate specificity of ten sortase homologs using libraries of synthetic peptide substrates.

Type

Text

Publisher

Western Washington University

OCLC Number

915140401

Digital Format

application/pdf

Genre/Form

Academic theses

Language

English

Rights

Copying of this thesis in whole or in part is allowable only for scholarly purposes. It is understood, however, that any copying or publication of this thesis for commercial purposes, or for financial gain, shall not be allowed without the author's written permission.

Available for download on Thursday, August 09, 2018

Included in

Chemistry Commons

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