MALDI-ToF Mass Spectrometry for Studying Noncovalent Complexes of Biomolecules

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Author(s) Mädler, Stefanie, Boeri Erba, Elisabetta, Zenobi, Renato
Publication Type Journal Items, Publication Status: Published
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Title MALDI-ToF Mass Spectrometry for Studying Noncovalent Complexes of Biomolecules
Author(s) Mädler, Stefanie
Boeri Erba, Elisabetta
Zenobi, Renato
Journal or Series Title Topics in current chemistry
Volume Number 331
Start Page 1
End Page 36
ISSN 0340-1022
1436-5049
Publisher Springer
Publication Place Berlin
Publication Date 2013
Keyword(s) Chemical crosslinking
First shot phenomenon
Intensity fading
MALDI matrix
SUPREX
Abstract Matrix-assisted laser desorption/ionization mass spectrometry (MALDI-MS) has been demonstrated to be a valuable tool to investigate noncovalent interactions of biomolecules. The direct detection of noncovalent assemblies is often more troublesome than with electrospray ionization. Using dedicated sample preparation techniques and carefully optimized instrumental parameters, a number of biomolecule assemblies were successfully analyzed. For complexes dissociating under MALDI conditions, covalent stabilization with chemical cross-linking is a suitable alternative. Indirect methods allow the detection of noncovalent assemblies by monitoring the fading of binding partners or altered H/D exchange patterns.
DOI 10.1007/128_2011_311
Document Type Article
Publication Status Published
Language English
Assigned Organisational Unit(s) 03430
Organisational Unit(s)
NEBIS System Number 000008416
Source Database ID FORM-1355152205
WOS-000321616300002
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@article{Mdlr2013,
  author = "M{\"{a}}dler, Stefanie and Boeri Erba, Elisabetta and Zenobi, Renato",
  title = "{M}{A}{L}{D}{I}-{T}o{F} {M}ass {S}pectrometry for {S}tudying {N}oncovalent {C}omplexes of {B}iomolecules",
  journal = "Topics in current chemistry",
  year = 2013,
  volume = "331",
  pages = "1--36",
}


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