Nucleotide-induced conformational changes of tetradecameric GroEL mapped by H/D exchange monitored by FT-ICR mass spectrometry

Here we employ hydrogen/deuterium exchange mass spectrometry (HDX-MS) to access E. coli chaperonin GroEL conformation. The ~800 kDa tetradecameric GroEL plays an essential role in the proper folding of many proteins. Previous studies of the structural dynamics of GroEL upon ATP binding have been inc...

Descripción completa

Detalles Bibliográficos
Autores principales: Zhang, Qian, Chen, Jin, Kuwajima, Kunihiro, Zhang, Hui-Min, Xian, Feng, Young, Nicolas L., Marshall, Alan G.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group 2013
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3570780/
https://www.ncbi.nlm.nih.gov/pubmed/23409238
http://dx.doi.org/10.1038/srep01247

Internet

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3570780/
https://www.ncbi.nlm.nih.gov/pubmed/23409238
http://dx.doi.org/10.1038/srep01247

Ejemplares similares