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Nuclear resonance spectrometer for applications of chemical structure elucidation, including small molecules and modern biological applications such as protein structure elucidation, protein interactions, of the analysis of post-translational modifications. The system consists of a superconducting magnet (14 Tesla), 1H/13C/15N/31P quadrupole probe head, sample changer for 24 samples, console (frequency generation, amplifier, lock, gradient unit), Temperature unit (-15 to 60 ° C), Linux Workstation, Ultra stabilized power supply (UPS for 11 min). The system can automatically measure sequentially up to 24 samples (typical for the elucidation of the chemical structure of small molecules) or highly complex experiments for the protein signal assignment and protein structure elucidation, extending over several days or weeks.
Prof. Dr. Chiara Cabrele
Preliminary experiments for biomolecules (e.g., "fingerprint" 1H-15N two-dimensional protein spectrum) to determine whether a protein is suitable for NMR binding studies and / or three-dimensional NMR structure determination.
Methods & Expertise for Research Infrastructure
The device is used for the investigation of biological systems such as proteins, peptides and oligosaccharides. The applications range from the structural confirmation of peptides (chemical structure) to the three-dimensional structure determination of proteins.
A focus is the mapping of protein interaction sites with binding partners to the protein sequence as well as the localization of the binding on the ligand side.
Another focus is on the detection of post-translational modifications.
Smaller tasks are the chemical structure elucidation of small molecules, e.g. purified unknown substances, or the confirmation of the identity of substances which were acquired either commercially or from co-operation partners.
Furthermore, the chemically working groups at the University of Salzburg (for example, Prof. Nicola Hüsing, Department of Chemistry and Physics of Materials) are supported by routine measurements (one-dimensional 1H and 13C spectra).
Allocation to Core Facility
Department of Chemistry and Physics of Materials, University of Salzburg
Wroclaw University of Science and Technology, Poland
Institute of Clinical Biochemistry, Hannover Medical School, Hannover, Germany
Department of Chemistry and Pharmacy, University of Regensburg, Germany
Institute of Microbiology, ETH Zurich, Switzerland
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
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
Maia ACD, Grimm C, Schubert M, Etl F, Gonçalves EG, Do Amaral Ferraz Navarro DM, Schulz S, Dötterl S
J. Chem. Ecol.
A New Family of Capsule Polymerases Generates Teichoic Acid-Like Capsule Polymers in Gram-Negative Pathogens
Litschko C, Oldrini D, Budde I, Berger M, Meens J, Gerardy-Schahn R, Berti F, Schubert M, Fiebig T
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
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
Two Distinct Conformations in Bet v 2 Determine Its Proteolytic Resistance to Cathepsin S
Soh WT, Briza P, Dall E, Asam C, Schubert M, Huber S, Aglas L, Bohle B, Ferreira F, Brandstetter H
Int. J. Mol. Sci. 18(10):E2156
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
A Secondary Structural Element in a Wide Range of Fucosylated Glycoepitopes
Aeschbacher T, Zierke M, Smieško M, Collot M, Mallet JM, Ernst B, Allain FH, Schubert M
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
Inhibition of delta-secretase improves cognitive functions in mouse models of Alzheimer's disease
Z. Zhang, O. Obianyo, E. Dall, Y. Du, H. Fu, X. Liu, S.S. Kang, M. Song, S.P. Yu, C. Cabrele, M. Schubert, X. Li, J.Z. Wang, H. Brandstetter, K. Ye
Nat. Commun. 8:14740
Dimerization of the fungal defense lectin CCL2 is essential for its toxicity against nematodes
S. Bleuler-Martinez, K. Stutz, R. Sieber, M. Collot, J.M. Mallet, M. Hengartner, M. Schubert, A. Varrot, M. Künzler
Structural basis for sulfation-dependent self-glycan recognition by the human immune-inhibitory receptor Siglec-8
J. M. Propster, F. Yan, B. Ernst, F.H.-T. Allain, M. Schubert
Proc. Natl. Acad. Sci. USA 113, E4170-9
Straightforward Solvothermal Synthesis toward Phase Pure Li2CoPO4F
J. Schoiber, R.J.F. Berger , J. Bernardi, M. Schubert, C. Yada, H. Miki, N. Husing
Crystal Growth & Design 16, 4999-5005
Crystal Growth & Design 16, 4999-5005