This is a very basic question, and I would be very happy, if you could share some of your experience with me. In my hands, GST by itself is always a dimeric protein (from size exclusion profiles), and the buffer conditions don't really seem to affect the dimer formation. I always assumed, that also the GST-fused proteins were dimers, but I found some papers that managed to show monomeric GST-fused proteins. What do you reckon?
Hi Paul, thank you for your suggestion, it is an interesting paper. Unfortunately, it does not answer my question because I would like to understand if papers reporting monomeric GST-fused proteinsdo actually make any sense. So still waiting for more feedback
If the fused protein, in a GST-fusion protein, interferes with the dimerization domain of GST, then the GST-fusion protein could be monomeric.
The dimeric nature of the traditional GST-tag could be a problem for my protein which is a dimer itself. The GST-tagged version seems to sort of polymerize (or aggregate in many very small aggregates), so I'm looking into mutations to monomerize the GST-tag. Here's an interesting paper:
http://www.jbc.org/content/283/47/32880.full
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