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Team:Virginia Commonwealth/Internal/Project ideas
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| - | 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 <nowiki>"~~~~"</nowiki> | + | 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 <nowiki>"~~~~"</nowiki> after it. |
==Systematic characterization of promotors== | ==Systematic characterization of promotors== | ||
===Overview=== | ===Overview=== | ||
| + | Significant knowledge gaps remain in the functional and dynamic characterization of several gene promotors, and engineering decisions depend on detailed quantitative information. | ||
===Comments=== | ===Comments=== | ||
| + | George, do you have any good papers about this? [[User:Chris.m.gowen|Chris.m.gowen]] 01:08, 22 April 2009 (UTC) | ||
==Development of thermostable enzymes== | ==Development of thermostable enzymes== | ||
| + | ===Overview=== | ||
| + | ===Comments=== | ||
==Extracellular enzyme scaffold== | ==Extracellular enzyme scaffold== | ||
Revision as of 01:08, 22 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 "~~~~" after it.
Contents |
Systematic characterization of promotors
Overview
Significant knowledge gaps remain in the functional and dynamic characterization of several gene promotors, and engineering decisions depend on detailed quantitative information.
Comments
George, do you have any good papers about this? Chris.m.gowen 01:08, 22 April 2009 (UTC)
Development of thermostable enzymes
Overview
Comments
Extracellular enzyme 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?
Organisms with cellulosomes
Clostridium thermocellum
C. acetobutylicum
