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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)
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
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
Journal Journal of Biomolecular NMR
Quellenangaben Volume: 59, Issue: 1, Pages: 1-14
Publishing Place Dordrecht
Reviewing status Peer reviewed
Institute(s) Institute of Structural Biology (STB)