MALDI LRF Mass spectrometry

University of Salzburg

Salzburg | Website

Large equipment

Short Description

The device consists of: Ion source for matrix-assisted laser desorption / ionization (MALDI), including pulsed ion extraction and variable ion extraction energy; solid state laser with 2000 Hz repetition rate; CCD-camera; time-of-flight (TOF)-mass analyzer for MS and MS/MS experiments in linear and reflector mode as well as positive and negative mode; detectors for linear and reflector mode; fully automated insertion of the target plate holder; uninterruptible power supply; control computer; control and evaluation software with permanent license for device control, data acquisition/-processing/-analysis and calibration.

Contact Person

Prof. Dr. Chiara Cabrele

Research Services

Mass analysis of peptides, proteins, DNA / RNA, carbohydrates, polymers

Methods & Expertise for Research Infrastructure

Identification and characterization of synthetic, isolated and recombinant peptides and intact proteins, RNA / DNA, carbohydrates, synthetic polymers, organometallic complexes

Allocation to Core Facility

Chemical and Structural Biology

Prof. Dr. Chiara Cabrele
Fachbereich Biowissenschaften, Schwerpunkt ACBN
0043 662 8044 7240
Please contact us via, or contact the responsible person for this section, mentioned in the contact field
Department of Biosciences, University of Salzburg
Department of Chemistry and Physics of Materials, University of Salzburg
Department of Chemistry and Pharmacy, University of Regensburg, Germany
International PhD Program "Immunity in Cancer and Allergy"
Thalhamer Josef (Projektleiter), Aberger Fritz, Brandstetter Johann, Duschl Albert, Ferreira Fatima, Gratz Iris, Greil Richard, Hartmann Tanja, Huber Christian, Risch Angela, Wessler Silja

Kofaktor- und Substratabhängige Aktivierung des Gerinnungsfaktors IXa
Brandstetter Johann

Christian Doppler Laboratory for Innovative Tools for the Characterization of Biosimilars
Huber christian (Sprecher); Brandstetter Johann, Cabrele Chiara, Gadermaier Gabriele, Stutz Hanno
CD Forschungsgesellschaft, Sandoz, Thermo Fisher Scientific, bmWFJ
A Novel FRET Peptide Assay Reveals Efficient Helicobacter Pylori HtrA Inhibition Through Zinc and Copper Binding
Bernegger S, Brunner C, Vizovišek M, Fonovic M, Cuciniello G, Giordano F, Stanojlovic V, Jarzab M, Simister P, Feller SM, Obermeyer G, Posselt G, Turk B, Cabrele C, Schneider G, Wessler S
Sci. Rep.
DOI: 10.1038/s41598-020-67578-2

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 30(3):686
DOI: 10.1105/tpc.17.00963

Structural analyses of Arabidopsis thaliana legumain γ reveal differential recognition and processing of proteolysis and ligation substrates
Zauner FB, Elsässer B, Dall E, Cabrele C, Brandstetter H
J. Biol. Chem. 293(23):8934
DOI: 10.1074/jbc.M117.817031

The Recombinant Inhibitor of DNA Binding Id2 Forms Multimeric Structures via the Helix-Loop-Helix Domain and the Nuclear Export Signal
Roschger C, Schubert M, Regl C, Andosch A, Marquez A, Berger T, Huber CG, Lütz-Meindl U, Cabrele C
Int. J. Mol. Sci. 19(4):E1105
DOI: 10.3390/ijms19041105

Complete NMR Assignment of Succinimide and Its Detection and Quantification in Peptides and Intact Proteins
Grassi L, Regl C, Wildner S, Gadermaier G, Huber CG, Cabrele C, Schubert M
Anal. Chem. 89(22):11962
DOI: 10.1021/acs.analchem.7b01645

Targeting of a Helix-Loop-Helix Transcriptional Regulator by a Short Helical Peptide
Roschger C, Neukirchen S, Elsässer B, Schubert M, Maeding N, Verwanger T, Krammer B, Cabrele C
ChemMedChem 12(18):1497
DOI: 10.1002/cmdc.201700305

Impact of the amino acid sequence on the conformation of side chain lactam-bridged octapeptides
Neukirchen S., Krieger V., Roschger C., Schubert M., Elsässer B., Cabrele C.
J. Pept. Sci. 23(7-8):587-596
DOI: 10.1002/psc.2997