Solubility and Conformational Studies of the Intrinsically Disordered HIV-1 Tat1-72 Protein
| dc.contributor.author | Babiak, Taras | |
| dc.contributor.examiningcommittee | Stetefeld, Jorg (Chemistry) Mark, Brian (Microbiology) | en |
| dc.contributor.supervisor | O'Neil, Joe (Chemistry) | en |
| dc.date.accessioned | 2011-04-20T15:42:24Z | |
| dc.date.available | 2011-04-20T15:42:24Z | |
| dc.date.issued | 2011-04-20T15:42:24Z | |
| dc.degree.discipline | Chemistry | en_US |
| dc.degree.level | Master of Science (M.Sc.) | en_US |
| dc.description.abstract | Tat1-72, is an intrinsically disordered protein at pH 4.1 as previously indicated by NMR chemical shifts and coupling constants, and confirmed by 15N-relaxation parameters. The presence of SDS elicits a conformational change to α-helicity in Tat1-72. In the presence of the non-ionic DDM detergent and zinc, Tat was found to be soluble at pH 4 when bound to TAR RNA; TAR binding also elicits a conformational shift to α-helicity in Tat1-72. The β-sheet content of Tat1-72 is increased in the presence of NaCl. In similar conditions, Tat1-72 aggregates stained with Congo Red displayed a yellow-green birefringence and a red-shift in the Congo Red absorbance that is typical of β-amyloid fibril. The web-based algorithm “WALTZ” identifies the majority of the Tat1-72 hydrophobic core region as amyloidogenic. The helical propensity of Tat1-72 in TFE was determined by two-dimensional NMR spectroscopy. | en |
| dc.description.note | May 2011 | en |
| dc.format.extent | 3258041 bytes | |
| dc.format.mimetype | application/pdf | |
| dc.identifier.uri | http://hdl.handle.net/1993/4594 | |
| dc.language.iso | eng | en_US |
| dc.rights | open access | en_US |
| dc.subject | HIV-1 | en |
| dc.subject | Tat | en |
| dc.subject | Intrinsically Disordered | en |
| dc.subject | Circular Dichroism | en |
| dc.subject | NMR | en |
| dc.title | Solubility and Conformational Studies of the Intrinsically Disordered HIV-1 Tat1-72 Protein | en |
| dc.type | master thesis | en_US |