Prediction and design of protein structures and interactions

Published on October 1, 2007 Reviewed on July 16, 2015   47 min

Other Talks in the Series: Protein Folding, Aggregation and Design

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Structural biology should be computable.
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It's been known for over 40 years that protein structures are completely determined by their amino acid sequences. For almost all protein structures and all protein-protein complexes, the experimentally observed structures and conformations are almost certain to correspond to global free energy minima. So, it should be possible to predict the structures of proteins and protein-protein complexes readily by identifying the global free energy minima for a polypeptide chain, in case of protein structure prediction, or identifying the global free energy minima for two proteins coming together, which will be the prediction of protein complexes problem. If we could do this, it would both be a fundamental test of our understanding of macromolecular and interactions, and it would also be huge practical relevance as the cost of determining protein structures computationally, would be a small fraction of the cost of current experimental methods such as X-ray crystallography, and NMR spectroscopy. But, as you know, today, structural biology is not computed, it is primarily experimental science. And what I'm going to tell you about today is progress towards making structural biology computable. The work I'm going to tell you about today is carried out
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Prediction and design of protein structures and interactions

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