Date: Thursday 17th of December at 12:00 in Askja room N-132
Title: Investigating protein disorder and interactions with high-field NMR and single-molecule FRET
Speaker: Dr. Louise Pinet, Associate Professor, ENS de Lyon, France
Abstract: Intrinsically disordered proteins play central roles in signaling by enabling dynamic, multimodal interactions that are inaccessible to structured domains alone. Here, we used solution NMR spectroscopy and single-molecule FRET (smFRET) to study disorder-driven mechanisms in cancer-relevant systems.
By NMR, we characterized the intrinsically disordered C-terminal tail of the receptor tyrosine kinase HER2, revealing transient structural features and novel interaction modes that expand its signaling repertoire beyond canonical phosphotyrosine recognition. We further investigated the adaptor protein Grb2, showing how its disordered linkers modulate domain coupling and enable multimodal engagement with HER2.
But NMR is not always the most suitable technique. To study nucleosome–H1–poly(ADP-ribose) assemblies, we used smFRET to resolve conformational heterogeneity and dynamic regulation of chromatin architecture.
Together, NMR and smFRET provide complementary views of intrinsically disordered proteins, linking residue-level information to long-range dynamics and functional plasticity in cancer.
Biography: Dr. Louise Pinet is an Associate Professor at ENS de Lyon (France). A chemist by training, she became an expert in NMR of disordered proteins during her PhD near Paris. She then expanded her expertise during her Postdoc in single-molecule FRET in Zürich (Switzerland). Now in Lyon, she is carrying out her research in the Very High Field NMR Center, studying disordered proteins in different biologically relevant contexts.
