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We make proteins in the lab, and we study them by biopysical methods, using solution NMR spectroscopy as the principal technique.


A brief overview of the most common techniques performed in our group:


Molecular cloning

  • PCR

  • DNA Electrophoresis

Protein expression

  • Expression in bacteria (E. coli)

  • Isotope labelling (2H, 15N 13C)

  • Specific labelling with different ILV precursors or single amino acid patterns.

Protein purification

  • A plethora of different types of chromatography (Affinity, Ion exchange, Size exclusion)

Biophysical characterisation

  • SDS-PAGE and Western-Blot


  • MS (in collaboration with the UZH Functional Genomic Center)

  • Kd determination (ITC, FP, MST)

  • NMR (our main analytical method)

Computational analysis:

  • Structure calculation and refinement (simulated annealing, using CYANA, XPLORPCR )

  • Structure prediction (Rosetta)

  • NMR-based analysis (assignments, CSPs, …)

  • Data structures analysis (python3, R, bash scripting)

A brief overview of our equipment:


  • Nanodrop

  • PCR Thermocycler

  • Incubators: Bioreactor (Sartoris stedim biostat A) and shaking flasks incubators (shakers)

  • Sonicator and French press

  • Centrifuges (Sorvall RC 6+ and RC5C) and ultracentrifuges (Sorvall Ultra and ThermoFisher WC Ultra 80)

  • Liquid chromatography: Äkta start, äkta prime, äkta purifier, Agilent 1260

  • MALS (Wyatt Technologies mini dawn treos)

  • ChemiDoc Imager (Bio-Rad)

  • Department NMR resources:  Bruker 400 (3), 500(3), 600(2), 700 MHz spectrometer

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