Cargando…
Probing Protein Denaturation during Size-Exclusion Chromatography Using Native Mass Spectrometry
[Image: see text] Size-exclusion chromatography employing aqueous mobile phases with volatile salts at neutral pH combined with electrospray-ionization mass spectrometry (SEC-ESI-MS) is a useful tool to study proteins in their native state. However, whether the applied eluent conditions actually pre...
Autores principales: | Ventouri, Iro K., Malheiro, Daniel B. A., Voeten, Robert L. C., Kok, Sander, Honing, Maarten, Somsen, Govert W., Haselberg, Rob |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
American Chemical
Society
2020
|
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7081181/ https://www.ncbi.nlm.nih.gov/pubmed/32107919 http://dx.doi.org/10.1021/acs.analchem.9b04961 |
Ejemplares similares
-
Capillary Electrophoresis: Trends and Recent Advances
por: Voeten, Robert L. C., et al.
Publicado: (2018) -
Characterizing
Non-covalent Protein Complexes Using
Asymmetrical Flow Field-Flow Fractionation On-Line Coupled to Native
Mass Spectrometry
por: Ventouri, Iro Konstantina, et al.
Publicado: (2023) -
Probing Polyester Branching by Hybrid Trapped Ion-Mobility
Spectrometry–Tandem Mass Spectrometry
por: Voeten, Robert L. C., et al.
Publicado: (2021) -
Affinity profiling of monoclonal antibody and antibody-drug-conjugate preparations by coupled liquid chromatography-surface plasmon resonance biosensing
por: Lakayan, Dina, et al.
Publicado: (2018) -
Rapid characterization of biotherapeutic proteins by size-exclusion chromatography coupled to native mass spectrometry
por: Haberger, Markus, et al.
Publicado: (2015)