Protein-protein interactions regulate signaling pathways within and between cells. They constitute the basis of the quaternary structure of multimeric proteins and represent one of the highest levels of structural organization in biology. Experimental techniques have provided atomic details of many protein-protein complexes. However, although it is feasible to extract common determinants of protein recognition from structural data, recent studies reported an extreme diversity of interaction modes. This is particularly true for transient associations that could be strengthen or weakened by specific cellular conditions, acting as an efficient regulatory mechanism. Here protein-protein interactions are classified and recurrent structural features of molecular recognition are illustrated. Moreover, metal-mediated associations are discussed to exemplify the role of cofactors in the stabilization of transient protein assemblies. In this view, the protein machinery mediating the activation of the nickel-enzyme urease from H. pylori is described. In particular, the activity of the metallo-chaperone UreE is analyzed in depth with respect to the association with its cognate UreG.
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Born in 1982 in Sassocorvaro, Italy. He achieved his Bachelor (2004) and M.S. Degree (2006) in Molecular and Industrial Biotechnology at the University of Bologna. He obtained his PhD in Biological, Biomedical and Biotechnological Science in April 2010. At present, he is a Junior Postdoc at Centre for Genomic Regulation (CRG) in Barcelona, Spain.
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Kartoniert / Broschiert. Etat : New. Dieser Artikel ist ein Print on Demand Artikel und wird nach Ihrer Bestellung fuer Sie gedruckt. Autor/Autorin: Bellucci MatteoBorn in 1982 in Sassocorvaro, Italy. He achieved his Bachelor (2004) and M.S. Degree (2006) in Molecular and Industrial Biotechnology at the University of Bologna. He obtained his PhD in Biological, Biomedical and Biot. N° de réf. du vendeur 4976516
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Taschenbuch. Etat : Neu. nach der Bestellung gedruckt Neuware - Printed after ordering - Protein-protein interactions regulate signaling pathways within and between cells. They constitute the basis of the quaternary structure of multimeric proteins and represent one of the highest levels of structural organization in biology. Experimental techniques have provided atomic details of many protein-protein complexes. However, although it is feasible to extract common determinants of protein recognition from structural data, recent studies reported an extreme diversity of interaction modes. This is particularly true for transient associations that could be strengthen or weakened by specific cellular conditions, acting as an efficient regulatory mechanism. Here protein-protein interactions are classified and recurrent structural features of molecular recognition are illustrated. Moreover, metal-mediated associations are discussed to exemplify the role of cofactors in the stabilization of transient protein assemblies. In this view, the protein machinery mediating the activation of the nickel-enzyme urease from H. pylori is described. In particular, the activity of the metallo-chaperone UreE is analyzed in depth with respect to the association with its cognate UreG. N° de réf. du vendeur 9783639311600
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Taschenbuch. Etat : Neu. Protein-Protein Interactions | A tool kit to puzzle out functional networks | Matteo Bellucci | Taschenbuch | Englisch | VDM Verlag Dr. Müller | EAN 9783639311600 | Verantwortliche Person für die EU: VDM Verlag Dr. Müller, Brivibas Gatve 197, 1039 RIGA, LETTLAND, customerservice[at]vdm-vsg[dot]de | Anbieter: preigu. N° de réf. du vendeur 107172349
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