Discussion of all aspects of biological molecules, biochemical processes and laboratory procedures in the field.
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Dr. M.L.P. Collins at the University of Wisconsin-Milwaukee has developed a new method for making large quantities of active, viable proteins using Rhodospirillum rubrum as a host. R. Rubrum is a bacterium that has traditionally been studied for its simple photosynthetic system, has demonstrated recent success in expressing high-yield protein.
To provide a brief overview, R. rubrum possesses the unique characteristic of forming an intracytoplasmic membrane (ICM) in response to membrane protein synthesis. The ICM is non-essential for growth and can incorporate foreign and over-expressed membrane proteins without disrupting normal cellular function. This characteristic has stimulated the expression of active and correctly folded membrane protein where other systems have failed.
In an attempt to gather additional testing data, the UWM Research Foundation would like to provide free protein expression kits to laboratories or universities that are having difficulties with their current method of producing large-scale proteins. Having limited resources, our researchers have only had the ability to test a number of proteins but thus far have seen exceptional promise. We currently have 8 other universities or companies using the new kit and are now ready to distribute to other participants. The link listed below provides a more detailed explanation of the testing process including the specific proteins currently being tested. You may also view Dr. Collin’s publication on her findings of using R. rubrum as a host. If you are interested in learning more about this new system or have any additional comments, you may email me at firstname.lastname@example.org.
Testing Kit Link
http://www.uwmresearchfoundation.org/ge ... -2013.aspx
Dr. Collin’s Publication
Butzin, N.C; Owen, H.A.; and M.L.P. Collins. 2010. A new system for heterologous expression of membrane proteins: Rhodospirillum rubrum. Protein Expression and Purification, 70: 88-94.
http://www4.uwm.edu/letsci/biologicalsc ... l_2010.pdf
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