ISBN: 3639311604

[EAN: 9783639311600], Neubuch, Publisher/Verlag: VDM Verlag Dr. Müller | A tool kit to puzzle out functional networks | Protein-protein interactions regulate signaling pathways within and… Meer...

[EAN: 9783639311600], Neubuch, Publisher/Verlag: VDM Verlag Dr. Müller | A tool kit to puzzle out functional networks | 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. | Format: Paperback | Language/Sprache: english | 210 gr | 144 pp, [PU: VDM Verlag Dr. Müller, Saarbrücken]<

2010, ISBN: 3639311604

[EAN: 9783639311600], Neubuch, [PU: VDM Verlag Dez 2010], This item is printed on demand - Print on Demand Neuware - Protein-protein interactions regulate signaling pathways within and be… Meer...

[EAN: 9783639311600], Neubuch, [PU: VDM Verlag Dez 2010], This item is printed on demand - Print on Demand Neuware - 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. 144 pp. Englisch<

ISBN: 9783639311600

[ED: Taschenbuch], [PU: VDM Verlag], Neuware - Protein-protein interactions regulate signaling pathways within and between cells. They constitute the basis of the quaternary structure of … Meer...

[ED: Taschenbuch], [PU: VDM Verlag], Neuware - 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., DE, [SC: 0.00], Neuware, gewerbliches Angebot, 222x154x14 mm, 144, [GW: 234g], PayPal, Offene Rechnung, Banküberweisung, Internationaler Versand<

2010, ISBN: 9783639311600

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[ED: Kartoniert / Broschiert], [PU: VDM Verlag Dr. Mueller], Dieser Artikel ist ein Print on Demand Artikel und wird nach Ihrer Bestellung fuer Sie gedruckt. Autor/Autorin: Bellucci Matte… Meer...

[ED: Kartoniert / Broschiert], [PU: VDM Verlag Dr. Mueller], 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 Biotechnol, DE, [SC: 0.00], Neuware, gewerbliches Angebot, Hardcover, 144, [GW: 222g], 1. Auflage, Banküberweisung, PayPal, [CT: Naturwissenschaft/Mathematik / Sonstiges - Naturwissenschaften]<

ISBN: 9783639311600

*Protein-Protein Interactions* - A tool kit to puzzle out functional networks / Taschenbuch für 58.99 € / Aus dem Bereich: Bücher, Wissenschaft, Biologie Medien > Bücher nein Buch (karton… Meer...

*Protein-Protein Interactions* - A tool kit to puzzle out functional networks / Taschenbuch für 58.99 € / Aus dem Bereich: Bücher, Wissenschaft, Biologie Medien > Bücher nein Buch (kartoniert) Hardcover;Naturwissenschaften, Medizin, Informatik, Technik;Biochemie, Biophysik, VDM Verlag Dr. Müller<