Stadler Andreas

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.
Furthermore, I will present selected SANS and NSE studies on the structure and dynamics of the intrinsically disordered myelin basic protein (1,2), of bovine serum albumin in its fully folded and different denatured states (3,4), and of different folding intermediates of apomyoglobin (5). Those chosen systems cover a broad range from intrinsically disordered proteins, to fully folded and partially folded intermediates up to denatured states. SANS experiments allowed us here to gain information of structural aspects, while NSE experiments gave valuable information on collective motions of the protein up to several hundred nanoseconds on the nanometre length-scale.

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.