Interaction Proteomics |
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Authors: | Maria Monti Stefania Orrù Daniela Pagnozzi Piero Pucci |
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Institution: | (1) CEINGE Biotecnologie Avanzate s.c.a r.l. Dipartimento di Chimica Organica e Biochimica, Università di Napoli Federico II, Complesso Universitario di Monte S. Angelo, via Cinthia 4, 80126 Napoli, Italy |
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Abstract: | The term proteome is traditionally associated with the identification of a large number of proteins within complex mixtures
originating from a given organelle, cell or even organism. Current proteome investigations are basically focused on two major
areas, expression proteomics and functional proteomics. Both approaches rely on the fractionation of protein mixtures essentially
by two-dimensional polyacrylamide gel electrophoresis (2D-gel) and the identification of individual protein bands by mass
spectrometric techniques (2D-MS). Functional proteomics approaches are basically addressing two main targets, the elucidation
of the biological function of unknown proteins and the definition of cellular mechanisms at the molecular level. In the cell
many processes are governed not only by the relative abundance of proteins but also by rapid and transient regulation of activity,
association and localization of proteins and protein complexes. The association of an unknown protein with partners belonging
to a specific protein complex involved in a particular process would then be strongly suggestive of its biological function.
The identification of interacting proteins in stable complexes in a cellular system is essentially achieved by affinity-based
procedures. Different strategies relying on this simple concept have been developed and a brief overview of the main approaches
presently used in functional proteomics studies is described. |
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Keywords: | Functional proteomics mass spectrometry protein– protein interactions affinity-based strategies |
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