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 proteins that have been evolutionary-optimized in the laboratory?