After Professor Bloch had been appointed director at the MPQ in 2008, he continued his doctoral work on “Single-atom-resolved imaging and single-spin addressing in an atomic Mott insulator” at the institute in Garching. In 2011 Christof Weitenberg received his doctoral degree from the Ludwig-Maximilians-Universität with “summa cum laude”. Subsequently, he became a fellow of the Alexander von Humboldt-Foundation and moved to the Laboratoire Kastler Brossel, Ecole Normale Supérieure (ENS) in Paris to the group of Jean Dalibard. This year he obtained a Marie Curie-Fellowship of the European Union.The central subject of his thesis was the detection and the manipulation of single atoms of an ultracold atomic quantum gas. The cold atoms are sitting in an artificial crystal of light, which is created by the superposition of several laser beams. They serve as a well-controlled model system for electrons in a solid-state material. Just like the electrons, the atoms can e.g. either freely move through the lattice or be pinned to their lattice site due to their mutual interaction. The latter case is called a Mott insulator.
Dr. Olivia Meyer-Streng | idw
MaterialVital Preis 2019 awarded for novel hydrogel wound dressings
05.09.2019 | Leibniz-Institut für Polymerforschung Dresden e. V.
Decoding cell communication
13.06.2019 | Friedrich-Alexander-Universität Erlangen-Nürnberg
To process information, photons must interact. However, these tiny packets of light want nothing to do with each other, each passing by without altering the...
Researchers from the Department of Atomically Resolved Dynamics of the Max Planck Institute for the Structure and Dynamics of Matter (MPSD) at the Center for Free-Electron Laser Science in Hamburg, the University of Hamburg and the European Molecular Biology Laboratory (EMBL) outstation in the city have developed a new method to watch biomolecules at work. This method dramatically simplifies starting enzymatic reactions by mixing a cocktail of small amounts of liquids with protein crystals. Determination of the protein structures at different times after mixing can be assembled into a time-lapse sequence that shows the molecular foundations of biology.
The functions of biomolecules are determined by their motions and structural changes. Yet it is a formidable challenge to understand these dynamic motions.
At the International Symposium on Automotive Lighting 2019 (ISAL) in Darmstadt from September 23 to 25, 2019, the Fraunhofer Institute for Organic Electronics, Electron Beam and Plasma Technology FEP, a provider of research and development services in the field of organic electronics, will present OLED light strips of any length with additional functionalities for the first time at booth no. 37.
Almost everyone is familiar with light strips for interior design. LED strips are available by the metre in DIY stores around the corner and are just as often...
Later during this century, around 2060, a paradigm shift in global energy consumption is expected: we will spend more energy for cooling than for heating....
Researchers from the Department of Atomically Resolved Dynamics of the Max Planck Institute for the Structure and Dynamics of Matter (MPSD) at the Center for Free-Electron Laser Science in Hamburg, the University of Potsdam (both in Germany) and the University of Toronto (Canada) have pieced together a detailed time-lapse movie revealing all the major steps during the catalytic cycle of an enzyme. Surprisingly, the communication between the protein units is accomplished via a water-network akin to a string telephone. This communication is aligned with a ‘breathing’ motion, that is the expansion and contraction of the protein.
This time-lapse sequence of structures reveals dynamic motions as a fundamental element in the molecular foundations of biology.
19.09.2019 | Event News
10.09.2019 | Event News
04.09.2019 | Event News
19.09.2019 | Power and Electrical Engineering
19.09.2019 | Physics and Astronomy
19.09.2019 | Event News