Abstract
Nuclear magnetic resonance (NMR) spectroscopy is a well suited method for the analysis of biomolecules in solution and provides unique insights into their structure, dynamics and function. Recent work has provided new approaches to determine surface-accessibility of biomolecules through the addition of freely soluble paramagnetic agents. This pushes the current limits towards more accurate and reliable structures, faster data acquisition and the detailed analysis of dynamic processes.
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Bernini A, Venditti V, Spiga O et al. (2009) Probing protein surface accessibility with solvent and paramagnetic molecules. Prog Nucl Magn Reson Spectrosc 54:278–289
Respondek M, Madl T, Göbl C et al. (2007) Mapping the orientation of helices in micelle-bound peptides by paramagnetic relaxation waves. J Am Chem Soc 129:5228–5234
Madl T, Bermel W, Zangger K (2009) Use of relaxation enhancements in a paramagnetic environment for the structure determination of proteins using NMR spectroscopy. Angew Chem Int Ed 48:8259–8262
Hartlmüller C, Göbl C, Madl T (2016) Prediction of protein structure using surface accessibility data. Angew Chem Int Ed 55:11970–11974
Hartlmüller C, Günther JC, Wolter AC et al. (2017) RNA structure refinement using NMR solvent accessibility data. Sci Rep 7:5393
Meyer NH, Tripsianes K, Vincendeau M et al. (2010) Structural basis for homodimerization of the Src-associated during mitosis, 68-kDa protein (Sam68) Qua1 domain. J Biol Chem 285:28893–28901
Göbl C, Focke-Tejkl M, Najafi N et al. (2017) Flexible IgE epitope-containing domains of Phl p 5 cause high allergenic activity. J Allergy Clin Immunol 140:1187–1191
Gong Z, Gu XH, Guo DC et al. (2017) Protein structural ensembles visualized by solvent paramagnetic relaxation enhancement. Angew Chem Int Ed 56:1002–1006
Öster C, Kosol S, Hartlmüller C et al. (2017) Characterization of protein–protein interfaces in large complexes by solid-state NMR solvent paramagnetic relaxation enhancements. J Am Chem Soc 139:12165–12174
Göbl C, Madl T, Simon B et al. (2014) NMR approaches for structural analysis of multidomain proteins and complexes in solution. Prog Nucl Magn Reson Spectrosc 80:26–63
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Christoph Göbl Jahrgang 1981. Chemiestudium an der Universität Graz, Österreich. 2008 Promotion in Biochemie und Molekularen Biowissenschaften an der Universität Graz, mit Aufenthalt an den National Institutes of Health, Bethesda, MD, USA. 2012–2016 Postdoc am Helmholtz Zentrum München. Seit 2016 Postdoc am Princess Margaret Cancer Centre in Toronto, Kanada.
Tobias Madl Jahrgang 1980. Chemie- und Physikstudium (Lehramt) an der Universität Graz, Österreich. 2007 Promotion, 2007–2010 Postdoc an der TU München und am Helmholtz Zentrum München. 2010–2011 Postdoc an der Universität Utrecht, Niederlande. 2012 APART-Stipendiat der Österreichischen Akademie der Wissenschaften. 2012–2016 BioSysNet und Emmy-Noether-Nachwuchsgruppenleiter an der TU München und am Helmholtz Zentrum München. Seit 2015 Assoziierter Professor an der Medizinischen Universität Graz, Österreich.
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Göbl, C., Madl, T. Entspannte Moleküle: NMR-Ober - flächen daten zur Strukturbestimmung. Biospektrum 24, 161–163 (2018). https://doi.org/10.1007/s12268-018-0898-5
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DOI: https://doi.org/10.1007/s12268-018-0898-5