Single Review on past events

It was an extremely interactive session that Malte Drescher gave in the last Jour Fixe of the winter term. To involve his audience in his presentation everyone received a classroom response system device. Malte used it to ask several questions related to his talk on “Molecular chameleons studied by ESR Spectroscopy”. Thus he got an impression of what his audience knows about chemistry in general and his research in particular.

Malte started by explaining basics: Proteins (the main object of his research) are macromolecules, and one molecule consists of several atoms. Then he asked his audience, what the term “protein chameleon” is referring to. He gave four possible answers. After thirty seconds the classroom response system showed clearly that many listeners knew or guessed the correct answer: A “protein chameleon” is a protein which can change its conformation. By means of the Electronic Spin Resonance (ESR) Spectroscopy the physicist can analyze the structure and dynamics of macromolecules; therefore a spin label is attached to the macromolecule under study. Based on the ESR spectrum you can measure the distance between two labels and find out more about the rotational mobility of the spin label. One main aim of the Fellow and his research group is to measure inter- and intramolecular distances in the nanometer range as well as dynamics on time scales between pico- and microseconds. 

The “benefits” of his studies Malte illustrated on the basis of the “protein chameleon” Alpha-Synuclein – an intrinsically disordered protein that is abundantly present in Lewy bodies (Parkinson‘s disease) and which physiological function is unknown. Investigating its intrinsic disorder can potentially help to find healing methods for Parkinson. So Malte´s group determined the structure the protein chameleon adapts upon interacting with membranes. In the end of his talk Malte mentioned further uses of the ESR Spectroscopy: to analyze the Human Telomeric DNA and In-Cell ESR.