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CONTROLLING THE FORM-DYNAMICS-FUNCTION RELATIONSHIP OF
PROTEINS WITH LIGHT ILLUMINATION
by
Shao-Chun Wang
____________________________________________________________________
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 Shao-Chun Wang
Object Description
| Title | Controlling the form-dynamics-function relationship of proteins with light illumination |
| Author | Wang, Shao-Chun |
| Author email | shaochuw@usc.edu |
| Degree | Doctor of Philosophy |
| Document type | Dissertation |
| Degree program | Chemical Engineering |
| School | Viterbi School of Engineering |
| Date defended/completed | 2008-03-26 |
| Date submitted | 2008 |
| Restricted until | Unrestricted |
| Date published | 2008-04-18 |
| Advisor (committee chair) | Lee, C. Ted |
| Advisor (committee member) |
Stephens, Philip J. Shing, Katherine |
| Abstract | The interaction of a light-responsive azobenzene-based surfactant ( azoTAB ) with proteins has been investigated as a means to photoreversibly control protein structure, dynamics, and function. AzoTAB undergoes a reversible photoisomeriztion upon exposure to appropriate wavelength of light, with the visible-light, trans isomer being more hydrophobic and, thus, inducing a greater degree of protein unfolding than the UV-light, cis form. AzoTAB is found to induce triggered and localized protein unfolding, measured directly in solution with small-angle neutron scattering (SANS) experiments, and to further influence the biological function and dynamics of proteins. For example, the relationship betweenphotoreversible changes in secondary and tertiary structure of BSA, found to exist as one of three discrete forms depending on the azoTAB concentration, has been examined. Similarly, photo-control of the form-function relationship of lysozyme has been studied. With azoTAB in the trans form under visible light a partially unfolded intermediate conformation of lysozyme with an exposed active site was found, while lysozyme was observed to refolded to a native-like structure upon UV illumination. In addition, enhanced dynamics within the partially-unfolded form of lysozyme were observed with neutron spin echo (NSE) measurements and thought to contribute to a nearly 8-fold enhancement in the enzyme activity compared to the native state. Combined, these results provide insight into a unique light-based method of controlling the complete structure-dynamics-function relationship of proteins. |
| Keyword | azobenzene; photoresponsive surfactant; protein conformation; neutron scattering; FTIR; light control |
| 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-m1132 |
| Rights | Wang, Shao-Chun |
| 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-Wang-20080418 |
| Archival file | uscthesesreloadpub_Volume44/etd-Wang-20080418.pdf |
Description
| Title | Page 1 |
| Full text | CONTROLLING THE FORM-DYNAMICS-FUNCTION RELATIONSHIP OF PROTEINS WITH LIGHT ILLUMINATION by Shao-Chun Wang ____________________________________________________________________ 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 Shao-Chun Wang |
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