Protein fold determined by paramagnetic magic-angle spinning solid-state NMR spectroscopy

Biomacromolecules that are challenging for the usual structural techniques can be studied with atomic resolution by solid-state nuclear magnetic resonance. However, the paucity of >5 Å distance restraints, traditionally derived from measurements of magnetic dipole-dipole couplings between protein...

Descripción completa

Detalles Bibliográficos
Autores principales: Sengupta, Ishita, Nadaud, Philippe S., Helmus, Jonathan J., Schwieters, Charles D., Jaroniec, Christopher P.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: 2012
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3335742/
https://www.ncbi.nlm.nih.gov/pubmed/22522262
http://dx.doi.org/10.1038/nchem.1299

Internet

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3335742/
https://www.ncbi.nlm.nih.gov/pubmed/22522262
http://dx.doi.org/10.1038/nchem.1299

Ejemplares similares