Wang, Lei
(2006)
The Denaturation of Cytochrome c and Cytochrome c as Peroxidase.
Master's Thesis, University of Pittsburgh.
(Unpublished)
Abstract
Conformational transitions of proteins play a crucial role in many biochemical and biophysical reactions. Understanding the conformational changes of a protein upon adsorption to a substrate is very important in biotechnology, e.g. the development of modern protein chip technology, biocompatibility of implants, and many other ones. This research program used cytochrome c, an electron carrier in the respiratory chain, as a model to probe how surface adsorption affects the folding of a protein. My work investigates the interaction of protein horse heart cytochrome c when it is electrostatically adsorbed or covalently attached onto a 1 nm thick monolayer film, which covers an Au surface. After changing the pH value of the solutions or adding the denaturants into the solutions, the conformation of cytochrome c changes and causes a change of the peak current of cyclic voltammgram. In addition, the denatured cytochrome c¡¯s peroxidase activity will be studied and compared with the peroxidase activity of microperoxidase-11.
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Details
Item Type: |
University of Pittsburgh ETD
|
Status: |
Unpublished |
Creators/Authors: |
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ETD Committee: |
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Date: |
28 September 2006 |
Date Type: |
Completion |
Defense Date: |
26 January 2006 |
Approval Date: |
28 September 2006 |
Submission Date: |
27 April 2006 |
Access Restriction: |
No restriction; Release the ETD for access worldwide immediately. |
Institution: |
University of Pittsburgh |
Schools and Programs: |
Dietrich School of Arts and Sciences > Chemistry |
Degree: |
MS - Master of Science |
Thesis Type: |
Master's Thesis |
Refereed: |
Yes |
Uncontrolled Keywords: |
cyclic voltammogram; cytochrome c; gold ball electode; hydrogen peroxide |
Other ID: |
http://etd.library.pitt.edu/ETD/available/etd-04272006-170820/, etd-04272006-170820 |
Date Deposited: |
10 Nov 2011 19:42 |
Last Modified: |
15 Nov 2016 13:42 |
URI: |
http://d-scholarship.pitt.edu/id/eprint/7684 |
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