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Dissertation/Thesis Abstract

Engineering Terpene Synthases and Antigen Binding by Phage Display
by Peterson, Katherine Mary, M.S., University of California, Irvine, 2011, 87; 1493762
Abstract (Summary)

Protein engineering explores and manipulates protein functions and molecular interactions to garner knowledge about and improve upon existing protein frameworks. Phage display technologies have been essential to the advancement of high-throughput analysis of such efforts. The research described herein explores the use of phage display for engineering thermostability and antigen binding. Chapter One overviews the expansive utility of protein engineering and phage display in creating novel proteins and cites examples of such efforts. Described in Chapter Two, three mutagenesis strategies were separately applied to the enzyme 5-epi-aristolochene synthase (TEAS) in efforts to engineer a thermostable terpene synthase. Chapter Three details how diverse phage-displayed antibody antigen-binding fragment (Fab) libraries can be used to select for antigen binding. The antibody Fab is responsible for molecular recognition, and as such, a synthetic Fab library was used to engineer binding to the human immunodeficiency virus class 1 (HIV-1) protein Nef. The selected Fab binds Nef with high affinity and specificity, and allows for future study of the protein and virus. Thus, this thesis investigates how phage display can be used to facilitate protein engineering.

Indexing (document details)
Advisor: Weiss, Gregory A.
Commitee: Luptak, Andrej, Van Vranken, David
School: University of California, Irvine
Department: Chemistry - M.S.
School Location: United States -- California
Source: MAI 49/06M, Masters Abstracts International
Subjects: Biochemistry
Keywords: Antigen binding fragments, HIV, Phage display, Protein engineering, Terpene
Publication Number: 1493762
ISBN: 978-1-124-66782-9
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