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Published on Apr 28, 2014
In this video our research group illustrates the folding of a newly synthesized protein in the bacterium Escherichia coli. The protein must navigate a crowded and complex environment to fold into its functional native state. It is assisted by a network of chaperones beginning with trigger factor which interacts with the nascent chain as it emerges from the ribosome. Then the DnaKDnaJGrpE and GroELES chaperone systems help untangle misfolded states and allow the protein to fold correctly. With support of a Pioneer grant we developed a computational program FoldEco that models protein folding in E. coli.