Intrinsically disordered proteins, IDPs, are characterized by a lack of stable tertiary structure. More recently it has been shown that ~30% of all proteins in eukaryotic organisms belong to this group of proteins, and that IDPs are involved in a large number of central biological processes and diseases. This discovery challenged the traditional protein structure paradigm, which stated that a specific well-defined structure was required for the correct function of a protein. Instead, in solution IDPs adopt a heterogenous ensemble of conformations, which can be altered by crowding and through interaction with membranes. Biochemical evidence has since shown that IDPs are functional, and that the lack of folded structures is related to their functions. There is a great interest in the research community in the structure-function relationship for IDPs. One hypothesis is that upon adsorption to surfaces, such as membranes, IDPs might adopt a more specific/folded structure, that modulates function. Hence, it is of interest to relate the properties of IDPs in solution with their properties in the adsorbed state and their interactions with biological membranes. To be able to obtain a molecular understanding of IDPs, it is useful to combine experimental solution-based techniques such as X-ray scattering, and neutron spectroscopy, with surface adsorption techniques such as neutron reflectivity, ellipsometry, and QCM-D. Additional insight into the effects of absorption can be gained by computer simulations using both atomistic and coarse-grained modelling. In this talk I will present our research regarding IDPs with respect to their structural, thermodynamical, and dynamical properties in solution, and the effects thereon upon adsorption to surfaces and lipid bilayers. 

From solution behaviour to interaction with lipid bilayers: Building a tool-box for understanding intrinsically disordered proteins

Macromolecular Chemistry: The Second Century

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ACS Spring 2020 National Meeting & Expo

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