Seminarium Zakładu Biofizyki

Intrinsically disordered proteins (IDPs) are an important class of biomolecules that regulate biological processes in higher organisms. The lack of a fixed spatial structure facilitates their regulatory functions and allows the efficiency of biochemical reactions to be controlled by temperature and the cellular environment. From a biophysical point of view, IDPs are biopolymers with a wide configuration state space and their actual conformation depends on the non-covalent interactions of their amino acid side chain groups at a given temperature and chemical conditions.

During this seminar I will discuss the pitfalls in interpreting the molecular properties of IDPs and how we can understand the hydrodynamic parameters of proteins as a function of their structural features. I will also present our recent results on the properties, interactions and propensity to liquid-phase separation of cytoplasmic proteins involved in the regulation of human gene expression, as well as extracellular coral acid-rich proteins responsible for biomineralisation in the skeletal organic matrix, studied by fluorescence correlation spectroscopy and confocal imaging.