Chemical and Structural Biology

University of Salzburg

Salzburg | Website

Core facility (CF)

Short Description

The core facility chemical & structural biology comprises the equipment for the preparation, purification, structural & functional characterization of biomolecules

- Synthesis robotics supports the chemical synthesis of peptides, different prokaryotic and eukaryotic cell expression system enable the biosynthesis of proteins and other biomolecules (PCR machines, cell incubators, centrifuges);
- chromatographic stations such as FPLC and HPLC allow the analytical and preparative purification of biomolecules;
- functional characterization is carried out by a spectrum of biophysical and biochemical techniques, including different optical spectroscopies (UV-VIS absorption spectrometer, fluorescence spectrometer, Fourier transform near infrared spectrometer, circular - dichroism spectrometer), static & dynamic light scattering, isothermal calorimeter, micro-thermophoresis, and enzymatic fluorescence-based assay;
-structural characterization is carried out by nano-liter crystallization and X-ray diffraction as well as NMR spectroscopy

Contact Person

Prof. Dr. Hans Brandstetter

Research Services

chemical peptide synthesis and purification
protein expression and purification
biomolecular quality control including homogeneity, activity, correct folding
enzymatic characterization for several enzymatic activities
biomolecular interaction, including binding affinity, binding enthalpy, binding entropy, ligand screening
binding epitope mapping
fold stability and melting temperature analysis
2d and 3d protein structure determination

Methods & Expertise for Research Infrastructure

The core facility Chemical and Structural Biology provides critical support for biomolecular studies at the Department of Biosciences. Specifically it provides infrastructure and expertise in
- peptide synthesis
- recombinant protein expression and purification
- peptide & protein quality assessment
- functional peptide and protein characterization
- 1d, 2d and 3d structure analysis


Prof. Dr. Hans Brandstetter
Fachbereich Biowissenschaften
0043 662 8044 7270
Please contact us via, or contact the responsible person for this section, mentioned in the contact field
Priority Program Allergy Cancer BioNano Research Centre (ACBN), University of Salzburg
Department of chemistry and physics of materials, University of Salzburg
University of Innsbruck
Medical University of Vienna
Technical University of Munich
University of Antwerpen
Shire Bioscience Vienna
Novo Nordisk Kopenhagen
Universidade de Lisboa
University of Massachusetts, Amherst
MPI Golm
Sanford-Burnham Institute La Jolla
University of Bielefeld
University of Cologne
Helmholtz Forschungszentrum Jülich
Emory University, Medical School (USA)
Max Planck Institute of Biochemistry, Martinsried
University Hospital Salzburg (SALK), Paracelsus Private Medical School (PMU), Salzburg
German Cancer Research Center (DKFZ), Heidelberg
Funktionelle Prinzipien der Legumain-Macrocypin Interaktion
Elfriede Dall

Mechanismus des bakteriellen Kollagenabbaus
Esther Schönauer

CD Labor für Biosimilar Charakterisierung
Christian Huber, Hans Brandstetter, Chiara Cabrele, Gabriele Gadermaier, Hanno Stutz
Christian Doppler Gesellschaft

Immunity in Cancer & Allergy (doctoral program )
Josef Thalhamer, Fritz Aberger, Hans Brandstetter, Albert Duschl, Fatima Ferreira, Iris Gratz, Richard Greil, Tanja Hartmann, Jutta Horejs-Höck, Christian Huber, Angela Risch, Josef Thalhamer, Silja Weßler

BM4SIT Bet v 1 Mutant for Specific Immuno Therapy
F. Ferreira, R. van Ree, L. Zuidmeer, C.M. van Drunen, D. van Egmond, E.C. de Jong, W.J. Fokkens, L. Aglas, P. Chrusciel, F. Stolz, et al.

Coagulation Factors
Hans Brandstetter
Novo Nordisk

Proteinsynthese nach Maß (Rare Disease Cluster Salzburg)
Hannelore Breitenbach-Koller
Land Salzburg
Crystal Structure of Plant Legumain Reveals a Unique Two-Chain State with pH-Dependent Activity Regulation
Zauner FB, Dall E, Regl C, Grassi L, Huber CG, Cabrele C, Brandstetter H.
Plant Cell

Analytical Cascades of Enzymes for Sensitive Detection of Structural Variations in Protein Samples
Hollerweger JC, Hoppe IJ, Regl C, Stock LG, Huber CG, Lohrig U, Stutz H, Brandstetter H.
Analytical Chemistry

Inhibition of delta-secretase improves cognitive functions in mouse models of Alzheimer's disease
Zhang Z, Obianyo O, Dall E, Du Y, Fu H, Liu X, Kang SS, Song M, Yu SP, Cabrele C, Schubert M, Li X, Wang JZ, Brandstetter H, Ye K.
Nature communications

Crystal structure of Pla l 1 reveals both structural similarity and allergenic divergence within the Ole e 1-like protein family
Stemeseder T, Freier R, Wildner S, Fuchs JE, Briza P, Lang R, Batanero E, Lidholm J, Liedl KR, Campo P, Hawranek T, Villalba M, Brandstetter H, Ferreira F, Gadermaier G.
Journal of Allergy and Clinical Immunology

Methylation of ribosomal RNA by NSUN5 is a conserved mechanism modulating organismal lifespan
Markus Schosserer, Nadege Minois, Tina B. Angerer, Manuela Amring, Hanna Dellago, Eva Harreither, Alfonso Calle-Perez, Andreas Pircher, Matthias Peter Gerstl, Sigrid Pfeifenberger, Clemens Brandl, Markus Sonntagbauer, Albert Kriegner, Angela Linder, Andreas Weinhäusel, Thomas Mohr, Matthias Steiger, Diethard Mattanovich, Mark Rinnerthaler, Thomas Karl, Sunny Sharma, Karl-Dieter Entian, Martin Kos, Michael Breitenbach, Iain B. H. Wilson, Norbert Polacek, Regina Grillari-Voglauer, Lore Breitenbach-Koller, and Johannes Grillari
Nature communications

The Human NADPH Oxidase, Nox4, Regulates Cytoskeletal Organization in Two Cancer Cell Lines, HepG2 and SH-SY5Y
Auer S, Rinnerthaler M, Bischof J, Streubel MK, Breitenbach-Koller H, Geisberger R, Aigner E, Cadamuro J, Richter K, Sopjani M, Haschke-Becher E, Felder TK, Breitenbach M.
Frontiers in Oncology