News

Ursula Keller wins “Swiss Nobel” Marcel Benoist Prize- for pioneering work in ultrafast lasers
MUST2022 Conference- a great success!
New scientific highlights- by MUST PIs Wörner, Chergui, and Richardson
FELs of Europe prize for Jeremy Rouxel- “Development or innovative use of advanced instrumentation in the field of FELs”
Ruth Signorell wins Doron prizefor pioneering contributions to the field of fundamental aerosol science
New FAST-Fellow Uwe Thumm at ETH- lectures on Topics in Femto- and Attosecond Science
International Day of Women and Girls in Science- SSPh asked female scientists about their experiences
New scientific highlight- by MUST PIs Milne, Standfuss and Schertler
EU XFEL Young Scientist Award for Camila Bacellar,beamline scientist and group leader of the Alvra endstation at SwissFEL
Prizes for Giulia Mancini and Rebeca Gomez CastilloICO/IUPAP Young Scientist Prize in Optics & Ernst Haber 2021
Nobel Prize in Chemistry awarded to RESOLV Member Benjamin List- for the development of asymmetric organocatalysis
NCCR MUST at Scientifica 2021- Lightning, organic solar cells, and virtual molecules
Dr. 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
NCCR MUST Office : ETHZ IQE/ULP-HPT H3 | Auguste-Piccard-Hof 1 | 8093 Zurich | E-Mail
The National Centres of Competence in Research (NCCR) are a research instrument of the Swiss National Science Foundation