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
Call for Papers in Thematic Issues
Catalytic C-H bond activation as a tool for functionalization of heterocycles
The major topic is the functionalization of heterocycles through catalyzed C-H bond activation. The strategies based on C-H activation not only provide straightforward formation of C-C or C-X bonds but, more importantly, allow for the avoidance of pre-functionalization of one or two of the cross-coupling partners. The beneficial impact of ...read more
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