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Betting on Protein Folding

NSF Award:

NSF PostDoctoral Research Fellowship in Biology  (O'Brien, Edward P)

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Researchers have developed a theoretical model that accurately predicts the probability that a protein will correctly fold into its biologically active form as a function of the rate at which it is synthesized inside cells.

The model, developed by Ed O'Brien and colleagues at the University of Cambridge, represents an important step forward in understanding and predicting how proteins fold inside cells and provides a framework for rationally engineering cells to boost the amount of successfully folded and functioning proteins. This will ultimately aid in biotechnology applications designed to synthesize large quantities of protein. The results from the model may also help the design of synthetic organisms that have properties beneficial to people.

To carry out processes essential to keeping a cell alive, proteins self-assemble into well-defined 3-D structures. The first place in the cell where such self-assembly can occur is on a ribosome, which synthesizes proteins from the genomic information encoded in an mRNA molecule. This process, referred to as co-translational folding, can be significantly affected by the rate at which the protein is synthesized. In some cases, if this rate is too fast, the newly synthesized protein may mis-fold, potentially leading to various disease states or cell death.

Image

  • a simulation of protein folding on a ribosome
Simulation shows protein folding (blue) on a ribosome.
Edward O'Brien, University of Cambridge

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