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Structural Dynamics of Intrinsically Disordered and Partially Folded Proteins
A characteristic property of intrinsically disordered and partially folded proteins is a large inherent molecular flexibility. In my talk, I will first introduce the methods of small-angle neutron scattering (SANS) and neutron spin-echo spectroscopy (NSE) that allow us to study structure and dynamics of those flexible proteins in solution.
In my talk, I will provide an illustrative overview what we can learn from those studies on the connection between protein folding and protein dynamics. In general, internal motions of the unfolded proteins could be interpreted using concepts derived from polymer theory. I will introduce here the relevant polymer models and discuss to which extent motions in those biopolymers can be described by classical polymer theory and what is the physical reason for observed differences to ideal polymer-behaviour. With progressing content of folded structure more complex motional patters appear in the proteins. I will illustrate how those motional patters can be interpreted using normal mode analysis and how they can be related to the biological function of the proteins.
Senior Scientist at JCNS-1, FZ Jülich, Germany
Andreas Stadler currently works at the Julich Centre for Neutron Science (JCNS-1), Forschungszentrum Jülich, Germany. Andreas does research in Biophysical Chemistry and Molecular Biophysics. He is also teaching Physical and Biophysical Chemistry at RWTH Aachen University. Current scientific projects are focused on the investigation of molecular dynamics and solution structures of intrinsically disordered and unfolded proteins in response to environmental conditions and on their interaction with biological membranes. Experimental methods being used are primarily neutron, X-ray and light scattering techniques. For the interpretation of the experimental data of unfolded and partially folded proteins analytical models derived from polymer-theory are being employed, while computer simulations based on available crystal structures can be used to decipher the functionally relevant motions of folded proteins.