Investigation of the first shot phenomenon in MALDI mass spectrometry of protein complexes

The Analyst ◽  
2007 ◽  
Vol 132 (3) ◽  
pp. 199 ◽  
Author(s):  
Arno Wortmann ◽  
Tatiana Pimenova ◽  
Sandra Alves ◽  
Renato Zenobi
Keyword(s):  
Mass Spectrometry ◽  
Protein Complexes ◽  
Maldi Mass Spectrometry

scholarly journals Binding Specificities of Nanobody•Membrane Protein Complexes Obtained from Chemical Cross-Linking and High-Mass MALDI Mass Spectrometry

2018 ◽  
Vol 90 (8) ◽  
pp. 5306-5313 ◽  
Author(s):  
Martin Köhler ◽  
Christoph Neff ◽  
Camilo Perez ◽  
Cyrill Brunner ◽  
Els Pardon ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Membrane Protein ◽  
Protein Complexes ◽  
Maldi Mass Spectrometry ◽  
High Mass ◽  
Cross Linking ◽  
Membrane Protein Complexes ◽  
Chemical Cross Linking

scholarly journals Liquid Native MALDI Mass Spectrometry for the Detection of Protein-Protein Complexes

2018 ◽  
Vol 29 (10) ◽  
pp. 1981-1994 ◽  
Author(s):  
Martine Beaufour ◽  
David Ginguené ◽  
Rémy Le Meur ◽  
Bertrand Castaing ◽  
Martine Cadene
Keyword(s):  
Mass Spectrometry ◽  
Protein Complexes ◽  
Maldi Mass Spectrometry

MALDI Mass Spectrometry of Dye−Peptide and Dye−Protein Complexes

1998 ◽  
Vol 70 (8) ◽  
pp. 1536-1543 ◽  
Author(s):  
Bekir Salih ◽  
Renato Zenobi
Keyword(s):  
Mass Spectrometry ◽  
Protein Complexes ◽  
Maldi Mass Spectrometry

Time-dependent cortisol turnover in tissues using stable isotope tracers and MALDI Mass Spectrometry (MS) sampling

2018 ◽  
Author(s):  
Shazia Khan ◽  
Diego F Cobice ◽  
Dawn EW Livingstone ◽  
C Logan Mackay ◽  
Scott P Webster ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Stable Isotope ◽  
Maldi Mass Spectrometry ◽  
Time Dependent ◽  
Stable Isotope Tracers ◽  
Isotope Tracers

Characterization of Grp78/BiP Protein Complexes in Skeletal Muscle Using Affinity Mass Spectrometry

2017 ◽  
Vol 2 (4) ◽  
Author(s):  
Dapeng Chen ◽  
◽  
Eva R. Chin ◽  
Keyword(s):  
Mass Spectrometry ◽  
Skeletal Muscle ◽  
Protein Complexes

Rapid Online Buffer Exchange: A Method for Screening of Proteins, Protein Complexes, and Cell Lysates by Native Mass Spectrometry

2019 ◽  
Author(s):  
Zachary VanAernum ◽  
Florian Busch ◽  
Benjamin J. Jones ◽  
Mengxuan Jia ◽  
Zibo Chen ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
High Speed ◽  
Structural Information ◽  
Protein Complexes ◽  
High Sensitivity ◽  
Native Mass Spectrometry ◽  
Structural Features ◽  
Consumer Products ◽  
Cell Lysates ◽  
Protein Expression And Purification

It is important to assess the identity and purity of proteins and protein complexes during and after protein purification to ensure that samples are of sufficient quality for further biochemical and structural characterization, as well as for use in consumer products, chemical processes, and therapeutics. Native mass spectrometry (nMS) has become an important tool in protein analysis due to its ability to retain non-covalent interactions during measurements, making it possible to obtain protein structural information with high sensitivity and at high speed. Interferences from the presence of non-volatiles are typically alleviated by offline buffer exchange, which is timeconsuming and difficult to automate. We provide a protocol for rapid online buffer exchange (OBE) nMS to directly screen structural features of pre-purified proteins, protein complexes, or clarified cell lysates. Information obtained by OBE nMS can be used for fast (<5 min) quality control and can further guide protein expression and purification optimization.

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