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Dynamics in the solid-state: perspectives for the investigation of amyloid aggregates,membrane proteins and soluble protein complexes
Authors:Rasmus Linser  Riddhiman Sarkar  Alexey Krushelnitzky  Andi Mainz  Bernd Reif
Affiliation:1. Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, 240 Longwood Ave, Boston, MA, 02115, USA
2. Department of Chemie, Munich Center for Integrated Protein Science (CIPSM), Technische Universit?t München (TUM), Lichtenbergstr. 4, 85747, Garching, Germany
3. Deutsches Forschungszentrum für Gesundheit und Umwelt (HMGU), Helmholtz-Zentrum München, Ingolst?dter Landstr. 1, 85764, Neuherberg, Germany
4. Institut für Physik – NMR, Martin-Luther-Universit?t Halle-Wittenberg, Betty-Heimann-Str. 7, 06120, Halle (Saale), Germany
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.
Keywords:
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