Kurzbeschreibung
NMR spectrometer for structural biology of biological macromolecules
Ansprechperson
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
Methoden & Expertise zur Forschungsinfrastruktur
NMR structure determination,
NMR screening,
NMR technique development
protein NMR,
NMR based structural biology of biological macromolecules
study of interactions
Nutzungsbedingungen nach Rücksprache - siehe Kontakt
Boehringer-Ingelheim
Neuropore
Neuropore
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
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
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.
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.