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Dynamics in the solid-state: perspectives for the investigation of amyloid aggregates, membrane proteins and soluble protein complexes

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Abstract

Aggregates formed by amyloidogenic peptides and proteins and reconstituted membrane protein preparations differ significantly in terms of the spectral quality that they display in solid-state NMR experiments. Structural heterogeneity and dynamics can both in principle account for that observation. This perspectives article aims to point out challenges and limitations, but also potential opportunities in the investigation of these systems.

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Acknowledgments

This work was performed in the framework of SFB-1035/Project-B07 (German Research Foundation, DFG). This research was supported by the Helmholtz-Gemeinschaft, and the DFG (Re1435). We are grateful to the Center for Integrated Protein Science Munich (CIPS-M) for financial support. RL acknowledges the Australian Research Council for financial support in terms of a Discovery Early Career Researcher Award.

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Authors and Affiliations

  1. Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, 240 Longwood Ave, Boston, MA, 02115, USA

    Rasmus Linser

  2. Department of Chemie, Munich Center for Integrated Protein Science (CIPSM), Technische Universität München (TUM), Lichtenbergstr. 4, 85747, Garching, Germany

    Riddhiman Sarkar, Andi Mainz & Bernd Reif

  3. Deutsches Forschungszentrum für Gesundheit und Umwelt (HMGU), Helmholtz-Zentrum München, Ingolstädter Landstr. 1, 85764, Neuherberg, Germany

    Riddhiman Sarkar, Andi Mainz & Bernd Reif

  4. Institut für Physik – NMR, Martin-Luther-Universität Halle-Wittenberg, Betty-Heimann-Str. 7, 06120, Halle (Saale), Germany

    Alexey Krushelnitzky

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  1. Rasmus Linser
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  2. Riddhiman Sarkar
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  3. Alexey Krushelnitzky
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  4. Andi Mainz
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  5. Bernd Reif
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Correspondence to Bernd Reif.

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Linser, R., Sarkar, R., Krushelnitzky, A. et al. Dynamics in the solid-state: perspectives for the investigation of amyloid aggregates, membrane proteins and soluble protein complexes. J Biomol NMR 59, 1–14 (2014). https://doi.org/10.1007/s10858-014-9822-6

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  • DOI: https://doi.org/10.1007/s10858-014-9822-6

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