, Volume 24, Issue 2, pp 161–163 | Cite as

Entspannte Moleküle: NMR-Ober - flächen daten zur Strukturbestimmung

  • Christoph Göbl
  • Tobias Madl
Open Access
Wissenschaft · Special: Proteinanalytik Proteinstruktur


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.


  1. [1]
    Bernini A, Venditti V, Spiga O et al. (2009) Probing protein surface accessibility with solvent and paramagnetic molecules. Prog Nucl Magn Reson Spectrosc 54:278–289CrossRefGoogle Scholar
  2. [2]
    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 129:5228–5234CrossRefPubMedGoogle Scholar
  3. [3]
    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 48:8259–8262CrossRefGoogle Scholar
  4. [4]
    Hartlmüller C, Göbl C, Madl T (2016) Prediction of protein structure using surface accessibility data. Angew Chem Int Ed 55:11970–11974CrossRefGoogle Scholar
  5. [5]
    Hartlmüller C, Günther JC, Wolter AC et al. (2017) RNA structure refinement using NMR solvent accessibility data. Sci Rep 7:5393CrossRefPubMedPubMedCentralGoogle Scholar
  6. [6]
    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 285:28893–28901CrossRefPubMedPubMedCentralGoogle Scholar
  7. [7]
    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 140:1187–1191CrossRefPubMedGoogle Scholar
  8. [8]
    Gong Z, Gu XH, Guo DC et al. (2017) Protein structural ensembles visualized by solvent paramagnetic relaxation enhancement. Angew Chem Int Ed 56:1002–1006CrossRefGoogle Scholar
  9. [9]
    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 139:12165–12174CrossRefPubMedPubMedCentralGoogle Scholar
  10. [10]
    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 80:26–63CrossRefPubMedGoogle Scholar

Copyright information

© Die Autoren 2018

Open Access This article is distributed under the terms of the Creative Commons Attribution 4.0 International License (, which permits use, duplication, adaption, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made.

Open access funding provided by Medical University of Graz, Austria.

Authors and Affiliations

  1. 1.Princess Margaret Cancer CentreTorontoKanada
  2. 2.Gottfried Schatz Research CenterMedizinische Universität GrazGrazÖsterreich

Personalised recommendations