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BP: Fachverband Biologische Physik

BP 41: Protein structure and dynamics I

BP 41.3: Vortrag

Donnerstag, 19. März 2015, 10:15–10:30, H 1058

Structural changes of proteins at interfaces — •Lars Schmüser1, Nadja Hellmann2, Mischa Bonn1, and Tobias Weidner11Max Planck Institute for Polymer Research, Ackermannweg 10, 55128 Mainz, Germany — 2Institute for Molecular Biophysics, Jakob Welder Weg 26, 55128 Mainz, Germany

Information about the 3D structure of proteins at interfaces is essential for understanding of interfacial biological mechanisms. Structural insight can aid the design of tailored proteins with specific functions, structures or binding sites. However, static snapshots of protein structure are insufficient to understand many protein functions, which arise from protein dynamics: Protein folding, reorientation and motion. A well-established tool to study static protein structures is X-ray crystallography. But with this method it is still challenging to follow protein conformational change, folding or refolding in real time. We use vibrational sum frequency generation spectroscopy (SFG) to follow conformational changes of proteins at interfaces. The aim is to combine time resolved SFG with molecular dynamics simulations to glean information about protein dynamics and intermediate structures at interfaces during folding. For a pump-SFG probe detection scheme, an optical trigger for conformational change is a core requirement. We will discuss the design, preparation and characterization of model protein films with optical triggers.

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DPG-Physik > DPG-Verhandlungen > 2015 > Berlin