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Tesi etd-01162006-134718


Tipo di tesi
Tesi di dottorato di ricerca
Autore
Alpi, Emanuele
URN
etd-01162006-134718
Titolo
Deciphering PDZ mediated protein complexes by Affinity Chromatography and Mass Spectrometry
Settore scientifico disciplinare
CHIM/06
Corso di studi
SCIENZE CHIMICHE
Commissione
relatore Prof. Salvadori, Piero
relatore Prof. Dente, Luciana
Parole chiave
  • PATJ
  • MS
  • MALDI peptide mapping
  • affinity chromatography
  • PDZ domains
Data inizio appello
07/03/2006;
Disponibilità
parziale
Data di rilascio
2046-03-07
Riassunto analitico
Small modular binding domains mediate protein-protein interactions by conferring specificity in multiprotein complex formation. The variability of PDZ (PSD-95/Dlg/ZO-1) domains primary sequences and the structural adaptability of their fold results in different binding modalities. PDZs generally bind to the target carboxyl terminus, but they can also bind to internal sequences of other PDZ or other interaction modules. The eight PDZ domains of the protein PATJ (Protein Associated to Tight Junctions) have been assayed with protein extracts by affinity chromatography followed by mass spectrometry in order to find their protein interactors. Fifteen different proteins were indentified and the interactions of some of them with the PDZ domains of PATJ were further investigated
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