Biophysicists at TUM, the Technische Universität München, have published the results of single-molecule experiments that bring a higher-resolution tool to the study of protein folding. How proteins arrive at the three-dimensional shapes that determine their essential functions – or cause grave diseases when folding goes wrong – is considered one of the most important and least understood questions in the biological and medical sciences. Folding itself follows a path determined by its energy landscape, a complex property described in unprecedented detail by the TUM researchers. In this week's issue of the Proceedings of the National Academy of Sciences (USA), they report taking hold of a single, zipper-like protein molecule and mapping changes in its energy landscape during folding and unfolding.

An Oscar in the Scientific and Engineering Awards category will be presented this year to TUM Adjunct Professor Reimar Lenz. The Academy of Motion Picture Arts and Sciences will honor the pioneer in the field of digital photography for his contribution to the development of the ARRISCAN film scanner. The scanner enables high-speed, high-precision, and high-resolution scanning of analog feature film stock. The Oscar will also be awarded to Michael Cieslinski and Bernd Brauner from the Munich-based ARRI group (Arnold & Richter Cine Technik), who worked with Professor Lenz on the development of the scanner.

How do plant ecosystems react to rising concentrations of the greenhouse gas CO2 in the atmosphere over the long term? This fundamental question is becoming increasingly pressing in light of global climate change. Researchers from the Chair of Grassland Science at the Technische Universität München (TUM) have now – for the first time worldwide – taken up this issue for grasslands. The scientists found their answers in two unlikely places: in horns of Alpine ibex from Switzerland and in 150-year-old hay from England.