Nuclear Magnetic Resonance Spectroscopy (NMR) is a very powerful technique to study the structure and the dynamics of proteins in solution. My group at the University of Zurich uses solution NMR techniques to study proteins of high biological relevance. In particular, we are interested in G-protein coupled receptors (GPCRs), a class of membrane-embedded proteins that are involved in the transduction of signals into cells. We use temperature-stabilized mutants and a variety of labeling techniques to study GPCRs in the membrane-mimicking micelles and nanodiscs. We are in addition studying folding of GPCRs by investigating structural properties and membrane topology of fragments of GPCRs.  
A second major area of our interest is in the study of protein folding. This comprises both soluble as well as membrane proteins. A collaboration with groups of the Department of Biochemistry here at UZH aims at developing proteins with antibody-like peptide-binding properties using Armadillo repeat proteins as scaffolds. This project comprises a lot of NMR-guided protein design/engineering and the application of various other biophysical (calorimetric as well as spectroscopic) techniques to investigate their properties.
Finally, we  study metallothioneins (MTs), a class of small cysteine-rich metalloproteins involved in heavy-metal detoxification. We are particularly interested in understanding how MTs in organisms have adapted structurally to variable contents of heavy metal pollutants during evolution.


If you are interested in our research I would be happy to hear about it and please contact me by email.

 

 

 

Important publications
  • M. Poms, P. Ansorge, L. Martinez-Gil, S. Jurt, D. Gottstein, K. Caroccia, L. Cohen, P. Güntert, I. Mingarro, F. Naider, O.Zerbe: NMR Investigation of Structures of GPCR Folding Intermediates, J. Biol. Chem.(2016), 291, 27170–2718.
  • R. Watson, M. Christen, C. Ewald, F. Bumback, C. Reichen, M. Mihajlovic, E. Schmidt, P. Güntert, A. Plückthun, A. Caflisch, O. Zerbe (2014): Spontaneous Self-Assembly of Engineered Armadillo Repeat Protein Fragments into a Folded Structure, Structure (2014), 22, 985-995.
  • C. Baumann, A. Beil. S. Jurt, M Niederwanger, O. Palacios, M. Capdevila, S. Atrian, R. Dallinger, O. Zerbe: Structural adaptation of a protein to increased metal stress: NMR structure of a marine snail metallothionein with an additional domain, Angew. Chem.Int. Ed. (2017), 56, 4617-4622 (hot paper).

Prof. Dr. Oliver Zerbe

Department of Chemistry
University of Zurich
Winterthurerstr. 190
CH-8057 Zürich
Telefon: +41-44-635 42 63
Telefax: +41-44-635 68 82
:oliver.zerbe@chem.uzh.ch

 

 


Last modified: May, 2017 (oz)