Thursday, June 07, 2007
An emerging area of biotechnology research is the study of non-natural protein folds. Just how
well has nature explored the possible structural elements that make up proteins? Has it found
all the useful ones, most of them, or very few of them? Using mRNA display and novel selection
methodologies, Dr. John Chaput’s lab has uncovered entirely new folds never seen in nature and
has shown they can function in catalysis. His group investigates the directed molecular
evolution of nonbiological proteins from large combinatorial libraries.
During this week's podcast, Dr. Chaput
talks about how he and his team are trying to mimic Darwinian evolution in the laboratory by
evolving proteins de novo. He details the goals of this research. Dubbed "synthetic evolution,"
he shows how this synthetic evolutionary technique improves on what nature has done in terms of
creating proteins. Dr. Chaput describes the process of actually evolving a new protein and
lists the types of molecular biological techniques he and his colleauges rely upon.He is
particularly interested in learning more about the evolution of protein folding and stability
and offers insights on how his research is shedding light on these two areas.
An important result of the research is that he and his group discovered that only two amino
acid changes in a protein sequence enhanced the binding, solubility and heat stability of one
of your evolutionary optimized proteins. He addresses the ramifications of this finding and
highlights the next steps in his team's research on the synthetic evolution of proteins.
Be sure to listen then return to the blog
to give your thoughts on the following question:
Which specific life-science applications do you believe are most promising for protiens that
have been evolutionary-optimized in the laboratory?
6/8/2007
in vitro evolution is always limited to the stringency applied during the selection, so, not surprisingly, there is additional work to do, since often the final use of the "non-biological" protein is in a "biological" application. Using natural systems, where phage display actually allows almost similar size libraries, misfolded and insoluble proteins will rarely occur, although, one must keep in mind these might be still a valuable intermediate towards the ultimate goal. For technical applications of enzymes elevated temperatures will be preferred and in vitro selections are not limited to ambient temperatures. For biological/therapeutic applications one must keep in mind that at least larger proteins must be produced in a biological system and will be used in biological systems, therefore in vivo selections will be of advantage, since they filter from the beginning for adequate variants.
7/2/2007
Non-Biological proteins could be of great significance in the are of Energy. Current enzymes used for mass conversion have shortcommings that could be address through the use of non-biological cathalists. The main issue with current enzymes used in mass conversion is efficiency. This method for the generation of enzymes could address one major issue: stability.
NOTICE: As such, the comments on this blog were, are, and will always be solely the opinions of the individuals leaving them. In no way does Genetic Engineering & Biotechnology News, GEN Publishing, Inc., or Mary Ann Liebert ,Inc. endorse, condone, agree with, sponsor, etc. these comments.
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