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 2021Dr. Brankica Janković, Hamm Group, Uni Zurich
Postdoc
Research: My postdoctoral research in a group of Prof. Peter Hamm focuses on investigation of protein-ligand interactions by infrared spectroscopy. Model system that we are currently interested in is non-covalent complex of ribonuclease S which represents enzymatically treated enzyme ribonuclease A from bovine pancreas. RNase S is produced by subtilisin cleavage of ribonuclease A at specific position and consists of tightly associated peptide S (1-20 aa) and protein S (21-124 aa) which poses full enzymatic activity. Dissociated peptide S has predominantly random coil conformation in solution, whereas alfa helical conformation is favored in the bound state to folded protein S. Our main aim is to obtain further insights in mechanism of peptide S - protein S binding by using different modified forms of peptide S. By covalently modifying peptide S, we will introduce a bridging photoswitchable azobenzene molecule which could allow us to perturb the structure in a controlled manner. This perturbation should lead to dissociation of the peptide S form the complex, and should allow us to monitor time-resolved changes of peptide S and protein S conformation upon unbinding. Incorporation of site-specific and sensitive infrared labels, either in peptide S or protein S, could provide even more site-specific and detailed information on conformational changes that occur.
CV Brankica Janković
Contact details
Postdoc
Research: My postdoctoral research in a group of Prof. Peter Hamm focuses on investigation of protein-ligand interactions by infrared spectroscopy. Model system that we are currently interested in is non-covalent complex of ribonuclease S which represents enzymatically treated enzyme ribonuclease A from bovine pancreas. RNase S is produced by subtilisin cleavage of ribonuclease A at specific position and consists of tightly associated peptide S (1-20 aa) and protein S (21-124 aa) which poses full enzymatic activity. Dissociated peptide S has predominantly random coil conformation in solution, whereas alfa helical conformation is favored in the bound state to folded protein S. Our main aim is to obtain further insights in mechanism of peptide S - protein S binding by using different modified forms of peptide S. By covalently modifying peptide S, we will introduce a bridging photoswitchable azobenzene molecule which could allow us to perturb the structure in a controlled manner. This perturbation should lead to dissociation of the peptide S form the complex, and should allow us to monitor time-resolved changes of peptide S and protein S conformation upon unbinding. Incorporation of site-specific and sensitive infrared labels, either in peptide S or protein S, could provide even more site-specific and detailed information on conformational changes that occur.
CV Brankica JankovićContact details
