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Large equipment

NMR Varian Inova 600

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University of Vienna

Wien | Website

Open for Collaboration

Short Description

NMR spectrometer for structural biology of biological macromolecules

Contact Person

Georg Kontaxis

Research Services

characterization of organic and biological samples,
screening and characterization of biological interactions,
chemical and biological analytics
structure determination,
customized research services,
method development

Methods & Expertise for Research Infrastructure

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

Terms of Use

Nutzungsbedingungen nach Rücksprache - siehe Kontakt

Cooperation Partners

Boehringer-Ingelheim
Neuropore

Reference Projects

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

Reference Publications

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.

Contact

Georg Kontaxis
Department für Strukturbiologie und Computational Biology
T: +43-1-4277-522 18
georg.kontaxis@univie.ac.at
http://homepage.univie.ac.at/georg.kontaxis/
http://www.mfpl.ac.at/research/scientific-facilities/nmr-facility.html

Location

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