Background: With the increase in the number of genome sequencing projects, there is a concomitant exponential growth in the number of protein sequences whose function is still unknown. Functional proteomics constitutes an emerging research area in the proteomic field whose approaches are addressed towards two major targets: the elucidation of the biological function of unknown proteins and the definition of cellular mechanisms at the molecular level. Methods: The identification of interacting proteins in stable complexes in vivo is essentially achieved by affinity-based procedures. The basic idea is to express the protein of interest with a suitable tag to be used as a bait to fish its specific partners out from a cellular extract. Individual components within the multi-protein complex can then be identified by mass spectrometric methodologies. Results and conclusions: The association of an unknown protein with partners belonging to a specific protein complex involved in a particular mechanism is strongly suggestive of the biological function of the protein. Moreover, the identification of protein partners interacting with a given protein will lead to the description of cellular mechanisms at the molecular level. The next goal will be to generate animal models bearing a tagged form of the bait protein.

Functional proteomics / Monti, Maria; Orru, S; Pagnozzi, D; Pucci, Pietro. - In: CLINICA CHIMICA ACTA. - ISSN 0009-8981. - STAMPA. - 357:2(2005), pp. 140-150. [10.1016/j.cccn.2005.03.019]

Functional proteomics.

MONTI, MARIA;PUCCI, PIETRO
2005

Abstract

Background: With the increase in the number of genome sequencing projects, there is a concomitant exponential growth in the number of protein sequences whose function is still unknown. Functional proteomics constitutes an emerging research area in the proteomic field whose approaches are addressed towards two major targets: the elucidation of the biological function of unknown proteins and the definition of cellular mechanisms at the molecular level. Methods: The identification of interacting proteins in stable complexes in vivo is essentially achieved by affinity-based procedures. The basic idea is to express the protein of interest with a suitable tag to be used as a bait to fish its specific partners out from a cellular extract. Individual components within the multi-protein complex can then be identified by mass spectrometric methodologies. Results and conclusions: The association of an unknown protein with partners belonging to a specific protein complex involved in a particular mechanism is strongly suggestive of the biological function of the protein. Moreover, the identification of protein partners interacting with a given protein will lead to the description of cellular mechanisms at the molecular level. The next goal will be to generate animal models bearing a tagged form of the bait protein.
2005
Functional proteomics / Monti, Maria; Orru, S; Pagnozzi, D; Pucci, Pietro. - In: CLINICA CHIMICA ACTA. - ISSN 0009-8981. - STAMPA. - 357:2(2005), pp. 140-150. [10.1016/j.cccn.2005.03.019]
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11588/204472
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