Abstract
Mass spectrometry is a very versatile technique which has become both a high-throughput and a research tool in the biosciences. In this review, methods of functional protein analysis are discussed from a perspective in clinical research. The basics of proteomics is introduced as well as the determination of post-translational modifications such as phosphorylation. The investigation of protein interactions involves the measurement of non-covalent complexes and small molecule ligands as well as bioaffinity mass spectrometry. Comparative analysis of sample profiles on specific surfaces is performed increasingly to distinguish disease-related changes.
Keywords: matrix-assisted laser desorption (maldi), ion detector, magnetic sector, capillary electrophoresis, nanospray, phosphorylation analysis, ion microprobe, isotope-ratio mass spectrometry, proteomics, acetylation
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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