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Team:Virginia Commonwealth/Internal/Project ideas
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(New page: <div id="header">{{Template:Team:Virginia_Commonwealth/Templates/Header}}</div> We can use this space to brainstorm project ideas. Go crazy with it, and feel free to make comments and su...)
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Revision as of 20:51, 21 April 2009
We can use this space to brainstorm project ideas. Go crazy with it, and feel free to make comments and suggestions to existing ideas. Be sure to sign comments by inserting "~~~~" before it.
Contents |
Systematic characterization of promotors
Development of thermostable enzymes
Extracellular enzyme scaffold scaffold
Overview
A cell-associated protein scaffold which could accommodate various enzymes or binding proteins can create a cellular assembly line by drastically reducing inefficiencies of product and reactant diffusion and by aligning binding sites to targets. This concept is what makes the cellulosome of Clostridium thermocellum and other organisms so efficient at breaking down cellulose. See the [http://www.springerlink.com/content/785bm9d7uugugrdn/ review] by Schwarz for an overview of this system. A protein known as scaffoldin is a consistent part of each cellulosome, and provides the basic structure to which each catalytic enzyme attaches. In many cases a cohesin module can bind a wide range of proteins to the scaffoldin, and a dockerin module binds the scaffoldin to the cell surface. If we could export the scaffoldin and a dockerin module to E. coli, it may be possible to add the cohesin domain to the non-catalytic regions of desirable enzymes and create a synthetic "reaction line."
Problem areas
- Protein folding may be quite different in E. coli, especially from thermophilic source organisms.
- The dockerin module binds to the cell wall of the gram positive source organisms, which ecoli of course doesn't have...
- Integrating a foreign cohesin domain into native enzymes is in the realm of protein engineering, with which I am not familiar
- Others?
