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PHOTOCONTROL OF PROTEIN CONFORMATION THROUGH THE USE OF
PHOTORESPONSIVE SURFACTANTS, INVESTIGATED BY SMALL ANGLE
NEUTRON SCATTERING
by
Andrea C. Hamill
A Dissertation Presented to the
FACULTY OF THE GRADUATE SCHOOL
UNIVERSITY OF SOUTHERN CALIFORNIA
In Partial Fulfillment of the
Requirements for the Degree
DOCTOR OF PHILOSOPHY
(CHEMICAL ENGINEERING)
May 2008
Copyright 2008 Andrea C. Hamill
Object Description
| Title | Photocontrol of protein conformation through the use of photoresponsive surfactants, investigated by small angle neutron scattering |
| Author | Hamill, Andrea C. |
| Author email | ahamill@usc.edu |
| Degree | Doctor of Philosophy |
| Document type | Dissertation |
| Degree program | Chemical Engineering |
| School | Viterbi School of Engineering |
| Date defended/completed | 2008-02-25 |
| Date submitted | 2008 |
| Restricted until | Unrestricted |
| Date published | 2008-03-06 |
| Advisor (committee chair) | Lee, C. Ted |
| Advisor (committee member) |
Roberts, Richard Bau, Robert |
| Abstract | A photoresponsive surfactant, azoTAB, is used to control protein structure. When azoTAB is combined with a protein, illumination with visible and UV light can be used to induce different protein conformational changes. A means to reversibly control the secondary and tertiary structure of two proteins, lysozyme and RNase A, has been developed. In the presence of azoTAB and under visible light illumination, the alpha-domain of lysozyme unfolds, forming a new folding intermediate. Lysozyme transitions from this intermediate back to its native state under UV light illumination. Similarly, in the presence of azoTAB and under visible light illumination, a swollen form of RNase A is observed, which also transitions back to its native state under UV light illumination. Additionally, a means to control the quaternary structure of alpha-chymotrypsin has been developed. The degree of self-association of lapha-chymotrypsin, which readily associates in aqueous solution, is controlled when combined with azoTAB and UV or visible light illumination. Under visible light, the associated form is a corkscrew hexamer. Under UV light, these corkscrews self-associate in a slightly offset manner, forming ropelike dodecamers. The dodecamers were found to be preamyloidal. A means to control the association of a well-known amyloid protein linked to Alzheimer s disease, amyloid-beta peptide, has been developed. When combined with azoTAB and illuminated with visible light, the association of amyloid-beta into fibrils is significantly delayed relative to the association of pure amyloid-beta. UV light can be used to trigger the fibril formation process. In all cases, Small Angle Neutron Scattering was the main tool used to investigate the various changes in protein structure. |
| Keyword | protein; surfactant; small angle neutron scattering |
| Language | English |
| Part of collection | University of Southern California dissertations and theses |
| Publisher (of the original version) | University of Southern California |
| Place of publication (of the original version) | Los Angeles, California |
| Publisher (of the digital version) | University of Southern California. Libraries |
| Type | texts |
| Legacy record ID | usctheses-m1043 |
| Rights | Hamill, Andrea C. |
| Repository name | Libraries, University of Southern California |
| Repository address | Los Angeles, California |
| Repository email | http://www.usc.edu/isd/libraries/services/ask_a_librarian/email/ |
| Filename | etd-Hamill-20080306 |
| Archival file | uscthesesreloadpub_Volume23/etd-Hamill-20080306.pdf |
Description
| Title | Page 1 |
| Full text | PHOTOCONTROL OF PROTEIN CONFORMATION THROUGH THE USE OF PHOTORESPONSIVE SURFACTANTS, INVESTIGATED BY SMALL ANGLE NEUTRON SCATTERING by Andrea C. Hamill A Dissertation Presented to the FACULTY OF THE GRADUATE SCHOOL UNIVERSITY OF SOUTHERN CALIFORNIA In Partial Fulfillment of the Requirements for the Degree DOCTOR OF PHILOSOPHY (CHEMICAL ENGINEERING) May 2008 Copyright 2008 Andrea C. Hamill |
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