SMBp Group Meeting: Anum Glasgow (Columbia)

3rd Floor Classroom/3-Flatiron Institute (162 5th Avenue)

3rd Floor Classroom/3-Flatiron Institute

162 5th Avenue


Speaker: Anum Glasgow (Columbia)


Topic: Identifying evolutionarily conserved conformational changes towards designing functional proteins

Abstract: Biological regulation ubiquitously depends on protein allostery, but the regulatory mechanisms are incompletely understood, especially in proteins that undergo ligand-induced allostery with few structural changes. We used hydrogen-deuterium exchange with mass spectrometry (HDX/MS) to map allosteric effects in paralogous proteins that have the same structural topologies, in their different functional states. We discovered evolutionarily conserved conformational changes that enable functional switching in the protein family, and we dissected the roles of oligomerization state and ligand chemistry in enabling or constraining the proteins’ structural and functional responses. We are interested in scaling up our approach to generate large datasets for machine learning towards predicting protein conformational landscapes for applications in functional protein design.

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