Thesis(M.A.)--Case Western Reserve University, 2010 / Title from PDF (viewed on 2010-01-28) Department of Psychology Includes abstract Includes bibliographical references and appendices Available online via the OhioLINK ETD Center

Thesis--Technischen Hochschule, Stuttgart. / Vita. Includes bibliographical references (p. 87-90).

Thesis (Ph. D.)--Columbia University, 1918. / Vita. Includes bibliographical references (p. 27).

Proefschrift--Groningen. / "Stellingen": 3 p. at end. Bibliographical foot-notes.

Thesis (Ph. D.)--University of Wisconsin--Madison, 1961. / Typescript. Vita. eContent provider-neutral record in process. Description based on print version record. Bibliography: leaves 137-141.

Some of the properties of the specific summation methods will be investigated, such as what type of divergent series a method can or cannot sum, if the insertion of zeros into a series does change the sum, and when different methods give the same sum for a series.

Thesis (Ph. D.)--Oregon State University, 1963. / Typescript. Includes bibliographical references (leaves 180-182). Also available on the World Wide Web.

Thesis (doctoral)--Georg-August-Universität zu Göttingen, 1920. / Vita. Includes bibliographical references (p. [53]-54).

The tautomerase superfamily (TSF) provides an excellent model system to study enzyme specificity, catalysis, and divergent evolution. trans-3-Cholroacrylic acid dehalogenase (CaaD), cis-3-chloroacrylic acid dehalogenase (cis-CaaD), and malonate semialdehyde decarboxylase (MSAD) are three TSF members that catalyze the final reactions in the degradation of the nematocide, 1,3-dichloropropene. All three enzymes have the TSF characteristic beta-alpha-beta fold and catalytic amino terminal proline (Pro-1). Both CaaD and cis-CaaD dehalogenate their respective isomers of 3-chloroacrylic acid yielding malonate semialdehyde. Subsequently, MSAD decarboxylates malonate semialdhyde resulting in acetaldehyde and CO2. Their catalytic and substrate specificities are exquisite considering they share three key and positionally conserved residues. As part of an effort to understand how such specificity evolved, a pre-steady-state kinetic analysis of CaaD was carried out. Alongside a similar study on cis-CaaD, a fluorescent mutant of CaaD was constructed that had minimal kinetic differences from the wild-type. The mutant was validated as an accurate fluorescent reporter of change in enzyme state that allowed for the reaction to be followed using stopped-flow methods. Stopped-flow fluorescence, rapid chemical quench data and ultraviolet spectroscopy were globally fit by computational simulation. The fit resulted in a kinetic mechanism for CaaD affording detailed information about the reaction, including measuring the rate of product release, the rate of chemistry, a previously unknown partially rate-limiting step associated with a conformational change, and the definition of binding constants for both products (MSA and Br-). In addition to the dehalogenation reaction, the reaction of the fluorescent mutant with a mechanism-based inhibitor, 3-bromopropiolate, was characterized. The values for the apparent rate of inhibition and potency were defined and estimates were determined for the values of the rate of chemistry and the release of bromide. The information gathered during these inhibition experiments was used to further refine the CaaD dehalogenation mechanism eliminating ambiguities present in the initial data set. Finally, the reactions of a cis-CaaD homologue, Cg10062 from Corynebacterium glutamicum were characterized. Cg10062 shares high sequence similarity (53%) and the same six critical active site residues as cis-CaaD, but Cg10062 has poor cis-CaaD activity. Moreover, Cg10062 dehalogenates both 3-chloroacrylic acid isomers. The reactions of Cg10062 with propiolate, 2-butynoate, and 2,3 butadienoate were investigated. Cg10062 functions as a hydratase/decarboxylase using propiolate generating malonate semialdehyde and acetaldehyde. Cg10062 catalyzes a hydration-dependent decarboxylation of propiolate as exogenously added malonate semialdehyde is not decarboxylated. With 2,3 butadienoate and 2-butynoate, Cg10062 functions as a hydratase and yields only acetoacetate. Mutations to the activating residues Glu114 and Tyr103 produced a range of results from a reduction in wild-type activity to a switch of activity. Possible intermediates for the hydration and decarboxylation products can be trapped as covalent adducts to Pro-1 when NaCNBH3 is incubated with certain combinations of substrate and mutant enzymes. Three mechanisms are presented to explain these findings along with the strengths and weaknesses of each mechanism in terms of being able to account for experimental observations. / text

Finding the approximate location of short read genome sequences by comparing them to an already available closely related organism's complete genome sequence is a challenging research issue. Predicting intron locations in the short form of mRNA called Expressed Sequence Tags (ESTs) and the variability of intron lengths are the major challenges. More specifically, finding the intron positions in an EST sequence by comparing it with a reference genome sequence is a time consuming task, as currently it is done manually. In my thesis, I designed a pipeline that can predict the intron positions in ESTs of non-model organisms. Initially, I compared the ESTs to the closest completely sequenced genome. The pipeline then finds the alignment of the ESTs, the reference genome sequence, and the coding region of the gene (known as Coding DNA Sequence or CDS) from the reference genome.