Structural studies of flagellar motors and uroporphyrinogen III synthase

Update item information
Publication Type dissertation
School or College School of Medicine
Department Biochemistry
Author Mathews, Michael A. A.
Contributor Tang, Hua Lucy; Blair, David F.; Ni, Jinsong; McCloskey, James A.
Title Structural studies of flagellar motors and uroporphyrinogen III synthase
Date 2001-08
Description The focus of this dissertation is structural evaluation of proteins. The first three chapters relate to the proteins of the bacterial flagellar motor. The final four chapters are pertinent to an enzyme within the porphyrin biosynthetic pathway. I have used the tools of molecular biology, biochemistry, and x-ray crystallography to probe these proteins. Through the design and cloning of mutants, as well as binding studies between mutant proteins, I have mapped the regions of the protein FliM that are important in binding to the other flagellar proteins FliG, FliN, and CheY. Analytical ultra-centrifugation has been used to look at the possible solution states of FliM and FliN and perhaps shed some light on their states before being incorporated into the motor. X-ray protein crystallography is being attempted to determine the atomic structure of several of these flagellar proteins to better understand their function and mechanism of action. X-ray crystallography was used to determine the atomic structure of the fourth enzyme in the porphyrin biosynthetic pathway, uroporphyrinogen III synthase. An introduction to this enzyme is presented in Chapter 4, an overview of the method of x-ray crystallography comprises Chapter 5, the structure and discussion of the enzyme enzyme is in Chapter 6, and future directions for this research are found in Chapter 7.
Type Text
Publisher University of Utah
Subject Aanalysis; Proteins; Microbiology
Subject MESH Flagella; Bacterial Proteins; Porphyrins
Dissertation Institution University of Utah
Dissertation Name PhD
Language eng
Relation is Version of Digital reproduction of "Single copy replication control is regulated by genes involved in ubiquitin metabolism in the yeast Saccharomyces cerevisia." Spencer S. Eccles Health Sciences Library. Print version of "Single copy replication control is regulated by genes involved in ubiquitin metabolism in the yeast Saccharomyces cerevisia." available at J. Willard Marriott Library Special Collection. QK3.5 1995 .S57.
Rights Management © Michael A.A. Mathews.
Format Medium application/pdf
Format Extent 4,734,378 bytes
Identifier undthes,5458
Source Original: University of Utah Spencer S. Eccles Health Sciences Library (no longer available).
Master File Extent 4,734,419 bytes
ARK ark:/87278/s6w097rr
Setname ir_etd
Date Created 2012-04-24
Date Modified 2021-05-06
ID 191289
Reference URL https://collections.lib.utah.edu/ark:/87278/s6w097rr