Date of Award
Master of Science (MS)
Markus W. Germann
Part One. X-ray crystallography has benefited from the synthetic introduction of selenium to different positions within nucleic acids by easing the solving of the phase problem. Interestingly, its addition to the 2' position of the ribose ring also significantly enhances crystal formation. This phenomenon was investigated to describe the effect of selenium-based and other 2' modifications to the ribose ring of nucleosides in solution, as well as the incorporation of the selenium-modified nucleotides into a helical structure. This work correlates the difference in conformation propensity between the selenium containing nucleosides and oligomers towards a rationale behind the enhanced crystal forming behavior. Part Two. Recombinant protein production is a critical tool in laboratories and industries, and inducing extracellular transport of these products to the culture medium shows potential for improving cases where the yields are not sufficient in quality or quantity. This review incorporates current practices and systems with future perspectives.
Thompson, Richard A., "Conformational Bias in 2'-Selenium-Modified Nucleosides and the Effect on Helical Structure and Extracellular Recombinant Protein Production: Current Systems and Applications" (2011). Chemistry Theses. Paper 37.