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

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)

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Open Access Green as soon as Postprint is submitted to ZB.

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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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Publication type Article: Journal article

Document type Scientific Article

Corresponding Author

Keywords Amyloid Fibrils ; Mas Solid-state Nmr ; Membrane Proteins ; Protein Dynamics ; Soluble Protein Complexes; Human Prion Protein; Angle-spinning Nmr; Perdeuterated Proteins; Phospholipid-bilayers; Rotational Diffusion; Backbone Dynamics; Coupled Receptor; Sensitivity Enhancement; Nuclear-polarization; Dipolar Couplings

ISSN (print) / ISBN 0925-2738

e-ISSN 1573-5001

Journal Journal of Biomolecular NMR

Quellenangaben Volume: 59, Issue: 1, Pages: 1-14

Publisher Springer

Publishing Place Dordrecht

Non-patent literature Publications

Reviewing status Peer reviewed

Institute(s) Institute of Structural Biology (STB)