Thesis (Ph.D.)--Tufts University, 2001. / Adviser: Clemens Richert. Submitted to the Dept. of Chemistry. Includes bibliographical references (leaves 228-235). Access restricted to members of the Tufts University community. Also available via the World Wide Web;

Thesis (M.S.)--University of Wisconsin--Madison, 1966. / Typescript eContent provider-neutral record in process. Description based on print version record. Includes bibliographical references (leaves 59-62)

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Three types of 2-alkenylthiazolines were designed and synthesized by a two-step method starting with 2-methylthiazoline and aromatic aldehydes, alkyl aldehydes and alkenyl aldehydes, respectively. Diels-Alder reactions of several 2-styryl-1,3-thiazolines with maleic anhydride in toluene were attempted. Expected Diels-Alder products were not observed or separated. Only starting materials were recovered. Several 2-alkenyl-1,3-thiazolines were successfully reacted with benzoyl chloride to form the N-benzoyl mono-substituted products. This is in sharp contrast with the di-benzoylation of 2-methylthiazoline reported previously by the Pittman group. 2-Methylbenzothiazole was reacted with different folds of aroyl chlorides. However, only di-aroylation products were observed even when a 1:1 2-methylbenzothiazole:aroyl chloride ratio was employed. Finally, N-methyl cyclic ketene N,O- and N,S-acetals were reacted with different alkylsulfonyl chlorides, respectively. Only di-substituted products were found in the N,O-acetal reacitons and only mono-substituted products were found in the N,S-acetal reactions even when different folds of sulfonyl chloride was employed.

The attachment of myristic acid to the N-terminal glycine residue of many eukaryotic and viral proteins is often essential for the acquisition of the protein's biological activity. Vaccinia virus (VV), the prototype member of the Poxviridae, expresses several myristylated proteins during the course of infection. Only one of these proteins, L1R, has been identified and characterized. Experiments were performed to identify and analyze four additional VV myristylproteins. These proteins were identified as the A-type inclusion protein (92 kDa), G9R (39 kDa), A16L (36 kDa), and E7R (17 kDa). The latter three proteins were shown to be myristylated on an N-terminal glycine residue. Additional studies demonstrated that both A16L and E7R are soluble proteins, unlike L1R, which is a constituent of the viral envelope. Furthermore, A16L could not be detected in either purified extracellular enveloped virus (EEV) or in intracellular mature virus (IMV). These are the two predominant forms of infectious virions produced during a VV infection. E7R was detected in EEV and, to a lesser extent, in IMV. Unlike the other proteins, the amino terminal sequence of the A-type inclusion protein did not fit the consensus sequence for N-myristylation (M-G-X-X-X-S/T/A/C/N), suggesting that it was internally myristylated. A combination of studies revealed that the protein is both myristylated and palmitylated. Addition of each acyl group could be separated temporally: myristylation occured co-translationally, while palmitylation occurred post-translationally. Genetic analyses of lysine doublets and arginine/lysine doublets within the A-type inclusion protein indicated that these sites are not utilized for myristylation. This is in contrast to the precursors of TNFoc and Ilia which are internally-myristylated on a lysine doublet. It is not clear why this protein would be both myristylated and palmitylated. Only class four palmitylproteins, such as the Src family of proteins, have been shown to be both myristylated and palmitylated. The A-type inclusion protein expressed by cowpox virus forms a large symmetrical matix in the cytoplasm of infected cells and generally contains mature virions. It is possible, therefore, that the function of acylation may be to stabilize the protein matrix or to assist in occlusion of enveloped virus particles. / Graduation date: 1998

Thèse de doctorat : Procédés biotechnologiques et alimentaires : INPL : 2006. / Titre provenant de l'écran-titre. Bibliogr.

Thesis (M.Sc.)--Memorial University of Newfoundland, 2000. / Bibliography: leaves 81-83.

Thesis (PhD)--University of South Australia, 2001.

Thesis (M.Sc. (Organic Chemistry))--Mahidol University, 1983. / A thesis submitted in partial fulfillment of the requirements for the degree of Master of Science (Organic Chemistry) in the Faculty of Graduate studies of Mahidol University, 1983.

Thesis (M.Sc. (Organic Chemistry))--Mahidol University, 1984.