University of Cambridge > > Biophysics Colloquia - (Chemistry) > “Disordered Proteins and their Dynamic Complexes in Biological Regulation”

“Disordered Proteins and their Dynamic Complexes in Biological Regulation”

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Intrinsic disorder is widely found in eukaryotic proteins involved in regulatory processes, with a dominant role in mediating protein recognition. Our view of protein complexes has been shaped by static crystal structures of folded proteins interacting via well-ordered, complementary surfaces. However, many important regulatory interactions may involve ‘dynamic’ complexes, as intrinsically disordered protein regions do not always stably fold upon binding. We have utilized NMR and SAXS data in conjunction with our computational algorithm ENSEMBLE to describe the disordered state ensembles of the cyclin dependent kinase inhibitor Sic1 and the CFTR regulatory® region, as well as their dynamic complexes. Comparison of our results to biological data provides insight into the unique modes of regulation mediated by such highly dynamic complexes.

This talk is part of the Biophysics Colloquia - (Chemistry) series.

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