LILBID and nESI : different native mass spectrometry techniques as tools in structural biology

  • Native mass spectrometry is applied for the investigation of proteins and protein complexes worldwide. The challenge in native mass spectrometry is maintaining the features of the proteins of interest, such as oligomeric state, bound ligands, or the conformation of the protein complex, during transfer from solution to gas phase. This is an essential prerequisite to allow conclusions about the solution state protein complex, based on the gas phase measurements. Therefore, soft ionization techniques are required. Widely used for the analysis of protein complexes are nanoelectro spray ionization (nESI) mass spectrometers. A newer ionization method is laser induced liquid bead ion desorption (LILBID), which is based on the release of protein complexes from solution phase via infrared (IR) laser desorption. We use both methods in our lab, depending on the requirements of the biological system we are interested in. Here we benchmark the performance of our LILBID mass spectrometer in comparison to a nESI instrument, regarding sample conditions, buffer and additive tolerances, dissociation mechanism and applicability towards soluble and membrane protein complexes.
Metadaten
Author:Oliver Peetz, Nils Hellwig, Erik Henrich, Julija Mezhyrova, Volker DötschORCiDGND, Frank BernhardORCiD, Nina MorgnerORCiDGND
URN:urn:nbn:de:hebis:30:3-501393
DOI:https://doi.org/10.1007/s13361-018-2061-4
ISSN:1879-1123
ISSN:1044-0305
Pubmed Id:https://pubmed.ncbi.nlm.nih.gov/30225732
Parent Title (English):Journal of the American Society for Mass Spectrometry
Publisher:Springer
Place of publication:New York [u. a.]
Document Type:Article
Language:English
Year of Completion:2018
Date of first Publication:2018/09/17
Publishing Institution:Universitätsbibliothek Johann Christian Senckenberg
Release Date:2019/04/25
Tag:Ion source; LILBID; Membrane proteins; Native mass spectrometry; Soluble proteins; nESI
Volume:30
Issue:1
Page Number:11
First Page:181
Last Page:191
Note:
Open Access: This article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made.
Note:
Correction erschienen in: Journal of The American Society for Mass Spectrometry, 30.2019, Nr. 3, S. 561
HeBIS-PPN:451289404
Institutes:Biochemie, Chemie und Pharmazie / Biochemie und Chemie
Exzellenzcluster / Exzellenzcluster Makromolekulare Komplexe
Wissenschaftliche Zentren und koordinierte Programme / Zentrum für Biomolekulare Magnetische Resonanz (BMRZ)
Dewey Decimal Classification:5 Naturwissenschaften und Mathematik / 54 Chemie / 540 Chemie und zugeordnete Wissenschaften
5 Naturwissenschaften und Mathematik / 57 Biowissenschaften; Biologie / 570 Biowissenschaften; Biologie
Sammlungen:Universitätspublikationen
Licence (German):License LogoCreative Commons - Namensnennung 4.0