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

Rasmus Linser; Riddhiman Sarkar; Alexey Krushelnitzky; Andi Mainz; Bernd Reif

doi:10.1007/s10858-014-9822-6

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

Rasmus Linser
, Riddhiman Sarkar
, Alexey Krushelnitzky
, Andi Mainz
, Bernd Reif

Publikation: Beitrag in Fachzeitschrift › Übersichtsartikel › Begutachtung

33 Zitate (Scopus)

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.

Originalsprache	Englisch
Seiten (von - bis)	1-14
Seitenumfang	14
Fachzeitschrift	Journal of Biomolecular NMR
Jahrgang	59
Ausgabenummer	1
DOIs	https://doi.org/10.1007/s10858-014-9822-6
Publikationsstatus	Veröffentlicht - Mai 2014
Extern publiziert	Ja

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10.1007/s10858-014-9822-6

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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 = "Amyloid fibrils, MAS solid-state NMR, Membrane proteins, Protein dynamics, Soluble protein complexes",

author = "Rasmus Linser and Riddhiman Sarkar and Alexey Krushelnitzky and Andi Mainz and Bernd Reif",

note = "Funding Information: Acknowledgments This work was performed in the framework of SFB-1035/Project-B07 (German Research Foundation, DFG). This research was supported by the Helmholtz-Gemeinschaft, and the DFG (Re1435). We are grateful to the Center for Integrated Protein Science Munich (CIPS-M) for financial support. RL acknowledges the Australian Research Council for financial support in terms of a Discovery Early Career Researcher Award.",

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doi = "10.1007/s10858-014-9822-6",

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AU - Linser, Rasmus

AU - Sarkar, Riddhiman

AU - Krushelnitzky, Alexey

AU - Mainz, Andi

AU - Reif, Bernd

N1 - Funding Information: Acknowledgments This work was performed in the framework of SFB-1035/Project-B07 (German Research Foundation, DFG). This research was supported by the Helmholtz-Gemeinschaft, and the DFG (Re1435). We are grateful to the Center for Integrated Protein Science Munich (CIPS-M) for financial support. RL acknowledges the Australian Research Council for financial support in terms of a Discovery Early Career Researcher Award.

PY - 2014/5

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N2 - 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.

AB - 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.

KW - Amyloid fibrils

KW - MAS solid-state NMR

KW - Membrane proteins

KW - Protein dynamics

KW - Soluble protein complexes

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

Abstract

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