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  Ion mobility–mass spectrometry as a tool to investigate protein–ligand interactions

Göth, M., & Pagel, K. (2017). Ion mobility–mass spectrometry as a tool to investigate protein–ligand interactions. Analytical and Bioanalytical Chemistry, 409(18), 4305-4310. doi:10.1007/s00216-017-0384-9.

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 Creators:
Göth, Melanie1, 2, Author           
Pagel, Kevin1, 2, Author           
Affiliations:
1Institute of Chemistry and Biochemistry, Freie Universität Berlin, BerlinGermany, ou_persistent22              
2Molecular Physics, Fritz Haber Institute, Max Planck Society, ou_634545              

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Free keywords: Ion mobility–mass spectrometry; Protein–ligand complexes; Native mass spectrometry; Noncovalent complexes; Catch and release; Collision-induced unfolding
 Abstract: Ion mobility–mass spectrometry (IM-MS) is a powerful tool for the simultaneous analysis of mass, charge, size, and shape of ionic species. It allows the characterization of even low-abundant species in complex samples and is therefore particularly suitable for the analysis of proteins and their assemblies. In the last few years even complex and intractable species have been investigated successfully with IM-MS and the number of publications in this field is steadily growing. This trend article highlights recent advances in which IM-MS was used to study protein–ligand complexes and in particular focuses on the catch and release (CaR) strategy and collision-induced unfolding (CIU).

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Language(s): eng - English
 Dates: 2017-05-132017-07
 Publication Status: Issued
 Pages: 6
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1007/s00216-017-0384-9
 Degree: -

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Title: Analytical and Bioanalytical Chemistry
  Abbreviation : Anal. Bioanal. Chem.
Source Genre: Journal
 Creator(s):
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Publ. Info: Heidelberg : Springer-Verlag
Pages: - Volume / Issue: 409 (18) Sequence Number: - Start / End Page: 4305 - 4310 Identifier: ISSN: 1618-2642
CoNE: https://pure.mpg.de/cone/journals/resource/111006469468428