Thesis (Ph.D.)--University of Nebraska-Lincoln, 2009. / Title from title screen (site viewed January 12, 2010). PDF text: 164 p. : col. ill. ; 5 Mb. UMI publication number: AAT 3359465. Includes bibliographical references. Also available in microfilm and microfiche formats.

Thesis (Ph. D.)--Northeastern University, 2008. / Title from title page (viewed Aug. 4, 2009). Graduate School of Arts and Sciences, Dept. of Biology. Includes bibliographical references.

Thesis (M.S. in Chemistry)--Washington State University, August 2009. / Title from PDF title page (viewed on Sept. 21, 2009). "Department of Chemistry." Includes bibliographical references (p. 60-66).

Thesis (M.S.)--Bowling Green State University, 2009. / Document formatted into pages; contains 50 p. : ill. (some col.) Includes bibliographical references.

Thesis (Ph.D.) - University of Queensland, 2005. / Includes bibliography.

Thesis (Ph. D.)--University of Texas at Austin, 2006. / Vita. Includes bibliographical references.

No description available.

published_or_final_version / abstract / Botany / Master / Master of Philosophy

published_or_final_version / Paediatrics and Adolescent Medicine / Master / Master of Philosophy

The thesis work contains two projects under the same umbrella. The first project is to provide a detailed analysis on the behavior of interfacial water molecules at protein-protein complexes, in this case focusing on homodimeric complexes, and to investigate their effect with respect to different residue types. For that reason the homodimeric data-set, which includes high-resolution (≤ 2.30 Å) X-ray crystal structures of 252 (140 Biological & 112 Non-biological) protein complexes was chosen to explore fundamental differences between interfaces that Nature has “engineered” vs. compared to interfaces found under man-made conditions. The data set was comprised of 5391 water molecules where a maximum of 4 Å from both interfacing proteins. Our analysis is applied a suite of modeling tools based on HINT, a program for hydropathic analysis developed in our laboratory. HINT is based on the experimental measurement of the hydrophobic effect. The second project is designed to explore various means of suppressing the expression of human genes that play critical role in HIV pathogenesis. To achieve this aim, a data set of Affymetrix Human HG Focus Target Array, which measures the expression levels of HIV seronegative and seropositive individuals in human PBMCs, was analyzed with Pathway Studio 9.0 software. This work gives insight into the elucidation of the important mechanisms of human proteins interactions in HIV seropositive individuals and their implications. Hence, we found the kind and types of microRNAs that are suppressing the human genes which have great role for HIV replication in a cell.