Supraleitender Magnet Oxford NMR 500

Universität Wien

Vienna | Website

Open for Collaboration

Kurzbeschreibung

NMR Varian Inova 500 inkl. Zubehör, Anlage Nr. 30003351 - RF-Konsole Varian Unity Inova 500.
NMR spectrophotometer for structural biology of biological macromolecules

Ansprechperson

Georg Kontaxis

Research Services

Derzeit werden keine Research Services für diese Forschungsinfrastruktur angeboten. Bei Interesse an einer Kooperation setzen Sie sich bitte mit Georg Kontaxis (georg.kontaxis@univie.ac.at) in Verbindung.

Methoden & Expertise zur Forschungsinfrastruktur

structural biology of biological macromolecules
NMR structure determination,
NMR screening,
NMR technique development
protein NMR,
NMR based structural biology of biological macromolecules
study of biological interactions

Nutzungsbedingungen

Nutzungsbedingungen nach Rücksprache - siehe Kontakt

Kooperationspartner

Boehringer-Ingelheim
Neuropore

Referenzprojekte

NMR Investigations of the hyperphosphorylated IDP Osteopontin
P – 28937 http://www.fwf.ac.at
Robert KONRAT http://www.mfpl.ac.at/mfpl-group/group/konrat.html

Structural Dynamics of IDPs probed by Cross-Correlated NMR Spin Relaxation
P – 28359 http://www.fwf.ac.at
Robert KONRAT http://www.mfpl.ac.at/mfpl-group/group/konrat.html

NMR Spectroscopy of Intrinsically Disordered Protein Complexes
P – 26317 http://www.fwf.ac.at
Robert KONRAT http://www.mfpl.ac.at/mfpl-group/group/konrat.html

NMR determination of Siderocalin ligand binding properties
P – 22125 http://www.fwf.ac.at
Robert KONRAT http://www.mfpl.ac.at/mfpl-group/group/konrat.html

Protein Dynamics and Adiabatic Fast Passage NMR Experiments
P – 20549 http://www.fwf.ac.at
Robert KONRAT http://www.mfpl.ac.at/mfpl-group/group/konrat.html

Referenzpublikationen

NMR analysis of the interaction of picornaviral proteinases Lb and 2A with their substrate eukaryotic initiation factor 4GII.
Aumayr M, Fedosyuk S, Ruzicska K, Sousa-Blin C, Kontaxis G, Skern T.
Protein Sci. 2015 Sep 19. doi: 10.1002/pro.2807.

IDPs: Less Disordered and More Ordered than Expected.
Konrat R., Biophys J. 2015 Oct 6;109(7):1309-11.
doi: 10.1016/j.bpj.2015.06.041.

NMR contributions to structural dynamics studies of intrinsically disordered proteins.
Konrat R., J Magn Reson. 2014 Apr;241:74-85.
doi: 10.1016/j.jmr.2013.11.011. Review.

Compensatory adaptations of structural dynamics in an intrinsically disordered protein complex.
Kurzbach D, Schwarz TC, Platzer G, Höfler S, Hinderberger D, Konrat R.,
Angew Chem Int Ed Engl. 2014 Apr 7;53(15):3840-3.
doi: 10.1002/anie.201308389. Epub 2014 Mar 6.

An improved algorithm for MFR fragment assembly.
Kontaxis G., J Biomol NMR. 2012 Jun;53(2):149-59.
doi: 10.1007/s10858-012-9632-7. Epub 2012 May 13.

Investigating the substrate specificity and oligomerisation of the leader protease of foot and mouth disease virus using NMR.
Cencic R, Mayer C, Juliano MA, Juliano L, Konrat R, Kontaxis G, Skern T.
J Mol Biol. 2007 Nov 2;373(4):1071-87.