Cargando…
Combining Chemical Cross-linking and Mass Spectrometry of Intact Protein Complexes to Study the Architecture of Multi-subunit Protein Assemblies
Proteins interact with their ligands to form active and dynamic assemblies which carry out various cellular functions. Elucidating these interactions is therefore fundamental for the understanding of cellular processes. However, many protein complexes are dynamic assemblies and are not accessible by...
Autores principales: | Haupt, Caroline, Hofmann, Tommy, Wittig, Sabine, Kostmann, Susann, Politis, Argyris, Schmidt, Carla |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MyJove Corporation
2017
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5755487/ https://www.ncbi.nlm.nih.gov/pubmed/29286378 http://dx.doi.org/10.3791/56747 |
Ejemplares similares
-
Oligomerisation of Synaptobrevin-2 Studied by Native Mass Spectrometry and Chemical Cross-Linking
por: Wittig, Sabine, et al.
Publicado: (2018) -
Cross-linking mass spectrometry uncovers protein interactions and functional assemblies in synaptic vesicle membranes
por: Wittig, Sabine, et al.
Publicado: (2021) -
Analyzing Protein Architectures and Protein-Ligand Complexes by Integrative Structural Mass Spectrometry
por: Ahdash, Zainab, et al.
Publicado: (2018) -
A combined quantitative mass spectrometry and electron microscopy
analysis of ribosomal 30S subunit assembly in E.
coli
por: Sashital, Dipali G, et al.
Publicado: (2014) -
Glycoproteomics of the Extracellular Matrix: A Method for Intact Glycopeptide Analysis Using Mass Spectrometry
por: Barallobre-Barreiro, Javier, et al.
Publicado: (2017)