NRSREVO

Re-Evolution of a Non Ribosomal Protein Synthethase

 Coordinatore THE CHANCELLOR, MASTERS AND SCHOLARS OF THE UNIVERSITY OF CAMBRIDGE 

 Organization address address: The Old Schools, Trinity Lane
city: CAMBRIDGE
postcode: CB2 1TN

contact info
Titolo: Ms.
Nome: Edna
Cognome: Murphy
Email: send email
Telefono: +44 1223 333543
Fax: +44 1223 332988

 Nazionalità Coordinatore United Kingdom [UK]
 Totale costo 0 €
 EC contributo 171˙867 €
 Programma FP7-PEOPLE
Specific programme "People" implementing the Seventh Framework Programme of the European Community for research, technological development and demonstration activities (2007 to 2013)
 Code Call FP7-PEOPLE-IEF-2008
 Funding Scheme MC-IEF
 Anno di inizio 2009
 Periodo (anno-mese-giorno) 2009-05-15   -   2011-05-14

 Partecipanti

# participant  country  role  EC contrib. [€] 
1    THE CHANCELLOR, MASTERS AND SCHOLARS OF THE UNIVERSITY OF CAMBRIDGE

 Organization address address: The Old Schools, Trinity Lane
city: CAMBRIDGE
postcode: CB2 1TN

contact info
Titolo: Ms.
Nome: Edna
Cognome: Murphy
Email: send email
Telefono: +44 1223 333543
Fax: +44 1223 332988

UK (CAMBRIDGE) coordinator 171˙867.62

Mappa


 Word cloud

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peptide    enzymes    enzyme    molecular    evolution    dealing    natural    directed    efficient   

 Obiettivo del progetto (Objective)

'Many peptide-based natural products of therapeutic importance are synthesised by nonribosomal peptide synthetases (NRPSs), large, multifunctional enzymes that operate as molecular assembly lines, by coupling and processing an extending chain of amino acid monomers. They are composed of numerous enzyme domains that carry out the steps of the bio-synthesis and provide an efficient route to natural products that are not easily accessible by synthetic chemistry. An efficient exploitation, however, still requires a much deeper understanding of the molecular basis of activity and specificity in NRPS enzymes. A set of approaches dealing with neutral drift, directed evolution and selective enzyme modification will be carried out on the model system TycA, taking advantage of knowledge and technologies available at the host institution as well as through a number of international collaborations and participation in the training programme of the FP7 network ENEFP (dealing with directed evolution of functional proteins).'

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