Deutsch
 
Hilfe Datenschutzhinweis Impressum
  DetailsucheBrowse

Datensatz

DATENSATZ AKTIONENEXPORT
Zur Ablage hinzufügen
  Lokale TagsFreigabegeschichteDetailsÜbersicht

Freigegeben
Zeitschriftenartikel

Multiple paramagnetic effects through a tagged reporter protein.

MPG-Autoren
/persons/resource/persons71698

Munari,  F.
Research Group of Protein Structure Determination using NMR, MPI for biophysical chemistry, Max Planck Society;

/persons/resource/persons59255

Wegstroth,  M.
Department of NMR-based Structural Biology, MPI for biophysical chemistry, Max Planck Society;

/persons/resource/persons14824

Becker,  S.
Department of NMR-based Structural Biology, MPI for biophysical chemistry, Max Planck Society;

/persons/resource/persons16093

Zweckstetter,  M.
Research Group of Protein Structure Determination using NMR, MPI for biophysical chemistry, Max Planck Society;

Externe Ressourcen

http://onlinelibrary.wiley.com/doi/10.1002/anie.201408615/pdf
(Verlagsversion)

Volltexte (beschränkter Zugriff)
Für Ihren IP-Bereich sind aktuell keine Volltexte freigegeben.
Volltexte (frei zugänglich)
Es sind keine frei zugänglichen Volltexte in PuRe verfügbar
Ergänzendes Material (frei zugänglich)

2088138_Suppl.pdf
(Ergänzendes Material), 10MB

Zitation

Camacho-Zarco, A. R., Munari, F., Wegstroth, M., Liu, W. M., Ubbink, M., Becker, S., et al. (2015). Multiple paramagnetic effects through a tagged reporter protein. Angewandte Chemie International Edition, 54(1), 336-339. doi:10.1002/anie.201408615.


Zitierlink: https://hdl.handle.net/11858/00-001M-0000-0024-BA06-3
Zusammenfassung
Paramagnetic effects provide unique information about the structure and dynamics of biomolecules. We developed a method in which the lanthanoid tag is not directly attached to the protein of interest, but instead to a reporter protein, which binds and then transmits paramagnetic information to the target. The designed method allows access to a large number of paramagnetic restraints and residual dipolar couplings produced from independent molecular alignments in high-molecular-weight proteins with unknown 3D structure