Rational design of protein aggregation

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• Prof. Frederic Rousseau, VIB (Belgium)
• Wednesday 10 February 2016, 10:30-11:30
• Department of Chemistry, Cambridge, Unilever lecture theatre.

If you have a question about this talk, please contact Jerome Charmet.

Protein aggregation is in large part determined by the presence of aggregation-prone segments in a protein sequence and their relation with the native structure. During this presentation I will illustrate how these aggregation-determining sequences can be engineered to increase aggregation resistance without affecting native protein structure. I will also show how these sequences can be harnessed to induce specific aggregation-induced loss-of-function phenotypes in bacteria, plants and mammalian cells. Both inhibiting and inducing aggregation could lead to useful biotechnological application. These exercises also inform on the evolutionary options allowing folded proteins to adapt solubility and on the sequence-dependence of protein aggregate toxicity.

This talk is part of the Biophysical Seminars series.

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