Stadler Andreas

 

Фамилия Имя Отчество:

Stadler Andreas

Место работы (учебы):

Forschungszentrum Jülich GmbH, Germany

Должность (курс обучения):

Senior Scientist

Название доклада:

Structural Dynamics of Intrinsically Disordered and Partially Folded Proteins

Анонс:

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.

Биография:

Senior Scientist at JCNS-1, FZ Jülich, Germany

RESEARCH INTERESTS

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.

CURRICULUM VITAE
1999 — 2005 studies of physics at TU Munich, Germany
2002 – 2003 studies of biophysics at University Paris, France
2003 Master in Molecular Biophysics, Prof. Dr. Catherine Etchebest, Paris
2005 Diploma in Physics, Prof. Dr. Fritz Parak, TU Munich
2006 — 2009 Ph.D. with Dr. Giuseppe Zaccai, Biophysics, ILL, Grenoble, France
2009 — 2011 PostDoc with Prof. Dr. Büldt, FZ Jülich, Germany
2011 — Staff scientist at JCNS-1, FZ Jülich, Germany
2019 Habilitation in Physical Chemistry, RWTH Aachen, Germany