Date:
Wed, 19/06/202412:00-13:30
Location:
Danciger B Building, Seminar room
Lecturer: Prof. Roy Beck-Barkai - Tel Aviv University
Abstract:
Short-range interactions and long-range contacts drive the 3D folding of structured proteins. The proteins’ structure has a direct impact on their biological function. However, nearly 40% of the eukaryotes proteome is composed of intrinsically disordered proteins (IDPs) and protein regions that fluctuate between ensembles of numerous conformations. Therefore, to understand their biological function, it is critical to depict how the structural ensemble statistics correlate to the IDPs’ amino acid sequence. In this talk I will share our recent results from small-angle X-ray scattering and time-resolved Förster resonance energy transfer (trFRET), studying the intramolecular structural heterogeneity of the neurofilament low intrinsically disordered tail domain (NFLt). Our findings show that while the average structure can be predicated based on minimal parameters and polymer physics coarse-grained theories, specific sequence motifs and context are needed to describe the protein’s ensemble of structures in solution. This emphasizes the necessity of advanced polymer theories to fully describe IDPs ensembles with the hope that it will allow us to model their biological function and dysfunction in diseased state.
Abstract:
Short-range interactions and long-range contacts drive the 3D folding of structured proteins. The proteins’ structure has a direct impact on their biological function. However, nearly 40% of the eukaryotes proteome is composed of intrinsically disordered proteins (IDPs) and protein regions that fluctuate between ensembles of numerous conformations. Therefore, to understand their biological function, it is critical to depict how the structural ensemble statistics correlate to the IDPs’ amino acid sequence. In this talk I will share our recent results from small-angle X-ray scattering and time-resolved Förster resonance energy transfer (trFRET), studying the intramolecular structural heterogeneity of the neurofilament low intrinsically disordered tail domain (NFLt). Our findings show that while the average structure can be predicated based on minimal parameters and polymer physics coarse-grained theories, specific sequence motifs and context are needed to describe the protein’s ensemble of structures in solution. This emphasizes the necessity of advanced polymer theories to fully describe IDPs ensembles with the hope that it will allow us to model their biological function and dysfunction in diseased state.