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Open Access Green möglich sobald Postprint bei der ZB eingereicht worden ist.
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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Publikationstyp
Artikel: Journalartikel
Dokumenttyp
Wissenschaftlicher Artikel
Schlagwörter
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
Zeitschrift
Journal of Biomolecular NMR
Quellenangaben
Band: 59,
Heft: 1,
Seiten: 1-14
Verlag
Springer
Verlagsort
Dordrecht
Nichtpatentliteratur
Publikationen
Begutachtungsstatus
Peer reviewed
Institut(e)
Institute of Structural Biology (STB)