Ursula Keller wins “Swiss Nobel” Marcel Benoist Prize
Farewell: the NCCR MUST ended 
MUST2022 Conference
New scientific highlights
FELs of Europe prize for Jeremy Rouxel
Ruth Signorell wins Doron prize
New FAST-Fellow Uwe Thumm at ETH
International Day of Women and Girls in Science
New scientific highlight
EU XFEL Young Scientist Award for Camila Bacellar,
Prizes for Giulia Mancini and Rebeca Gomez Castillo
Nobel Prize in Chemistry awarded to RESOLV Member Benjamin List
Hans Jakob Wörner invited to give the „New Horizons Solvay Lectures” 
Unusual keynote talk at an international scientific conference
NCCR MUST at Scientifica 2021Peter Hamm
December 18, 2009Peter Hamm, Professor of Physical Chemistry, University of Zurich received an ERC Advance Grant in "Physical Sciences and Engineering".
DYNALLO: Towards a Dynamical Understanding of Allostery
Allostery is a fundamental concept Nature uses to regulate the affinity of a certain substrate to an active site of a protein by binding a ligand to a distant allosteric site. Within this project, experimental tools are designed to gain an atomistic, dynamical understanding of the conformational transitions that give rise to allostery. The problem is approached from two distinctively different directions:
- Tools are developed to initiate conformational transitions of proteins that per se are not photoswitchable, in order to mimic allosteric transitions. To that end, two amino acid side chains of an allosteric protein are crosse-linked with a photo-switchable azobenzene-moiety to initiate a conformational transition similar to ligand binding. Ultrafast infrared spectroscopy, augmented with isotope and chemical labelling, is employed to time-resolve the conformational transition.
- Furthermore, a frequently expressed hypothesis will be experimentally tested, according to that allosteric and active site communicate by exchange of vibrational energy. To that end, versatile approaches are designed that allow one to locally deposit vibrational energy at essentially any site in a protein (e.g. through pumping of an optical chromophore that undergoes ultrafast internal conversion), and to detect its appearance at any other site by using vibrational transitions as local thermometers. Thereby, a network of connectivity in a given protein can be mapped out.
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