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

Datensatz

DATENSATZ AKTIONENEXPORT

Zur Ablage hinzufügen

Lokale TagsFreigabegeschichteDetailsÜbersicht

Freigegeben

Zeitschriftenartikel

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

MPG-Autoren

/persons/resource/persons129267

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

Externe Ressourcen

http://link.springer.com/content/pdf/10.1007%2Fs10858-014-9822-6.pdf
(Verlagsversion)

Volltexte (beschränkter Zugriff)

Für Ihren IP-Bereich sind aktuell keine Volltexte freigegeben.

Volltexte (frei zugänglich)

1977443.pdf
(Verlagsversion), 3MB

Ergänzendes Material (frei zugänglich)

Es sind keine frei zugänglichen Ergänzenden Materialien verfügbar

Zitation

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.

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

Zusammenfassung

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.