Thesis (M.S.)--Oregon State University, 1999. / Typescript (photocopy). Includes mounted photographs. Includes bibliographical references (leaves 77-86). Also available on the World Wide Web.

Thesis (M. Sc.)--University of Canterbury, 2008. / Typescript (photocopy). Includes bibliographical references (leaves 124-131). Also available via the World Wide Web.

Thesis (M. Phil.)--Hong Kong University of Science and Technology, 2004. / Includes bibliographical references (leaves 52-58). Also available in electronic version. Access restricted to campus users.

Thesis (Ph. D.)--University of Hong Kong, 1999. / Includes bibliographical references (leaves 120-142).

Thesis (Ph. D.)--Florida State University, 2004. / Advisor: Dr. Michael Chapman, Florida State University, College of Arts and Sciences, Dept. of Chemistry and Biochemistry. Title and description from dissertation home page (viewed Sept. 15, 2005). Document formatted into pages; contains vi, 76 pages. Includes bibliographical references.

Thesis (Ph. D.)--University of Hong Kong, 2005. / Title proper from title frame. Also available in printed format.

This study compared the effects of whey and casein on plasma AA, nitrogen balance (NBAL), glutathione and performance in dieting athletes. Twenty cyclists consumed 40 g·d-1 whey (WHEY) or casein (CAS) for 3 wk. On d 18 – 21 subjects restricted intake to 20 kcal·kg-1·d-1 plus protein supplement. Apparent NBAL was estimated on d 18 – 21 while postabsorptive and 2 h postprandial plasma AA were measured on d 14 and 21. On d 1, 15 and 22 subjects performed an exercise performance test and provided blood for glutathione analysis. Both groups experienced similar negative NBAL (CAS = -19.7 ± 1.4 g, WHEY = -21.4 ± 2.7 g) during energy restriction. There were trends towards a reduction in performance during energy restriction (p = 0.073) and an interaction of group with day (p = 0.072). There were significant main effects of state (postabsorptive = 34.5 ± 2.4 µM, postprandial = 37.1 ± 3.0 µM; p = 0.038) and day (d 14 = 33.8 ± 2.2 µM, d 21 = 37.8 ± 3.2 µM; p = 0.008) on plasma cysteine. There was a significant interaction of state and day on glutamine (p = 0.002), as levels increased 1.3% from postabsorptive to postprandial measurements on d 14, but decreased 4.2% on d 21. The absolute change in postabsorptive cysteine from d 14 to d 21 was correlated with NBAL (r = 0.766, p = 0.01) in CAS but not in WHEY. Plasma glutamine did not correlate with NBAL in either group. / Master of Science

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Proteins containing selenocysteine (selenoproteins) have been found to exist in organisms from all domains of life. Selenoproteins are important for many in vivo processes such as the removal of reactive oxygen containing species (ROS), redox disulfide shuffling reactions, and pro-hormone activation. Structurally and functionally analogous to cysteine, selenocysteine's lower pKa appears to be the defining chemical difference between these two amino acids. Using a single-molecule electrical recording technique, rate constants for the reaction of selenocysteine with small molecule disulfides were obtained over a pH range of 6 - 10. Analogous single molecule ~riments carried out ~ .. - using cysteine, revealed that, after correcting for the ratio of selenolate to selenol and thiolate to thiol based on the pKa of each amino acid, the nuc1eophilicity of selenocysteine was comparable to that of cysteine. The selenium atom of the selenylsulfide bond was found to be substantially more electrophilic than a sui fur atom of the analogous disulfide bond and the leaving group ability of the selenolate of selenocysteine compared to the thiolate of cysteine were found to be comparable. Another biologically relavant interaction that occurs in vivo is the reaction between selenocysteine and organoarsenic (Ill) molecules. It is known that arsenic (Ill) compounds are toxic to organisms, and that this toxicity stems from the ability to coordinate to the thiol and selenol groups of the cysteine and selenocysteine residues within proteins. The reaction of selenocysteine with an organoarsenic species was investigated at the single molecule level over the pH range 6.5 - 8.5. By carrying out an analogous reaction between cysteine and the organoarsenic (Ill) species, it was found that selenocysteine and cysteine exhibit similar reaction rates. The organoarsenic reagent could exist in a range of different protonation states in solution and it was concluded that the rate of reaction was governed by the equilibrium of the arsenic molecule, where only some of the forms were reactive towards the selenocysteine and cysteine groups.