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

Linser, R.; Sarkar, R.; Krushelnitzky, A.; Mainz, A.; Reif, B.

doi:10.1007/s10858-014-9822-6

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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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Linser, R.
Research Group of Solid-State NMR-2, MPI for Biophysical Chemistry, Max Planck Society;

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Citation

Linser, R., Sarkar, R., Krushelnitzky, A., Mainz, A., & Reif, B. (2014). Dynamics in the solid-state: Perspectives for the investigation of amyloid aggregates, membrane proteins and soluble protein complexes. Journal of Biomolecular NMR, 59(1), 1-14. doi:10.1007/s10858-014-9822-6.

Cite as: https://hdl.handle.net/11858/00-001M-0000-0018-9F0C-C

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.