Abstract
Mass spectrometry has been used to study noncovalent protein interactions. Two typical ionizations permit the analysis of fragile biomolecules : matrix assisted laser desorption ionization (MALDI) and electrospray ionization (ESI). The gentleness of these techniques allows the detection of intact noncovalent complexes by mass spectrometry. However, the analysis success depends on the sample preparation and the instrumental parameter tuning both in MALDI-MS as well as in ESI-MS. ESI-MS seems to be the best analytical tool for this study as shown by the large number of published articles. Mass spectrometry becomes more and more attractive to obtain rapidly information about multimeric structures and interaction between host and guest.
Keywords: protein complexes, biochemical pathways, fab (fast atom bombardment), noncovalent complexes
Current Organic Chemistry
Title: Biological Noncovalent Complexes By Mass Spectrometry
Volume: 9 Issue: 3
Author(s): J. Hardouin and C. M. Lange
Affiliation:
Keywords: protein complexes, biochemical pathways, fab (fast atom bombardment), noncovalent complexes
Abstract: Mass spectrometry has been used to study noncovalent protein interactions. Two typical ionizations permit the analysis of fragile biomolecules : matrix assisted laser desorption ionization (MALDI) and electrospray ionization (ESI). The gentleness of these techniques allows the detection of intact noncovalent complexes by mass spectrometry. However, the analysis success depends on the sample preparation and the instrumental parameter tuning both in MALDI-MS as well as in ESI-MS. ESI-MS seems to be the best analytical tool for this study as shown by the large number of published articles. Mass spectrometry becomes more and more attractive to obtain rapidly information about multimeric structures and interaction between host and guest.
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Cite this article as:
Hardouin J. and Lange M. C., Biological Noncovalent Complexes By Mass Spectrometry, Current Organic Chemistry 2005; 9 (3) . https://dx.doi.org/10.2174/1385272053369114
DOI https://dx.doi.org/10.2174/1385272053369114 |
Print ISSN 1385-2728 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5348 |
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