MEMSEMBLE

Assembling biomembranes: fundamentals of membrane transporter folding and creation of synthetic modules

 Coordinatore KING'S COLLEGE LONDON 

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 Nazionalità Coordinatore United Kingdom [UK]
 Totale costo 2˙312˙389 €
 EC contributo 2˙312˙389 €
 Programma FP7-IDEAS-ERC
Specific programme: "Ideas" implementing the Seventh Framework Programme of the European Community for research, technological development and demonstration activities (2007 to 2013)
 Code Call ERC-2011-ADG_20110310
 Funding Scheme ERC-AG
 Anno di inizio 2012
 Periodo (anno-mese-giorno) 2012-05-01   -   2017-04-30

 Partecipanti

# participant  country  role  EC contrib. [€] 
1    UNIVERSITY OF BRISTOL

 Organization address address: TYNDALL AVENUE SENATE HOUSE
city: BRISTOL
postcode: BS8 1TH

contact info
Titolo: Ms.
Nome: Sarah
Cognome: Everett-Cox
Email: send email
Telefono: +44 117 9289678
Fax: +44 117 9298383

UK (BRISTOL) beneficiary 566˙947.00
2    KING'S COLLEGE LONDON

 Organization address address: Strand
city: LONDON
postcode: WC2R 2LS

contact info
Titolo: Mr.
Nome: Paul
Cognome: Labbett
Email: send email
Telefono: +44 2078488184
Fax: 442078000000

UK (LONDON) hostInstitution 1˙745˙442.00
3    KING'S COLLEGE LONDON

 Organization address address: Strand
city: LONDON
postcode: WC2R 2LS

contact info
Titolo: Prof.
Nome: Paula Jane
Cognome: Booth
Email: send email
Telefono: +44 20 7836 5454
Fax: 442078000000

UK (LONDON) hostInstitution 1˙745˙442.00

Mappa


 Word cloud

Esplora la "nuvola delle parole (Word Cloud) per avere un'idea di massima del progetto.

artificial    assembly    theme    lipid    lacy    probe    bilayer    synthetic    protein    ribosomes    membrane    transition    proteins    biophysical    biology    translational    construction    co    folding    studied    tuneable   

 Obiettivo del progetto (Objective)

'Self-assembly is a hallmark of Biology. We are far from a complete understanding of this natural assembly, which in turn limits our ability to mimic biological construction in the bioengineering of tuneable synthetic systems. This proposal addresses the major challenge of membrane protein folding. Here, I intend to make a step change to my pioneering biophysical studies and investigate co-translational membrane protein folding. A central feature will be the creation of synthetic systems to probe key events in co-translational folding, as the protein folds in the membrane whilst emerging from the ribosome. An ambitious target is to make these systems tuneable, which will provide a new tool for the fabrication of membrane proteins and artificial cells in Synthetic Biology. The assembly of a tuneable artificial module that affords control over membrane protein synthesis is unprecedented. I focus on the ubiquitous superfamily of major facilitator proteins, namely the best studied family member, lactose permease, LacY. This proposal has state of the art biophysical mechanistic studies at its core, which interleave into Cell and Synthetic Biology. There are two themes: Theme 1. Determination of fundamental membrane protein folding parameters: folding transition states and lipid control Phi-value analysis will be used to probe the folding transition state of LacY; the first such analysis of a multi-domain membrane protein. Lipid parameters that control LacY folding will be quantified, including bilayer asymmetry using novel droplet interface bilayer methods. Theme 2: construction of tuneable synthetic co-translational folding systems Engineered ribosomes and translocon insertion machinery will be incorporated and LacY folding will be controlled. Translation will be regulated or halted using mutant ribosomes, arrest sequences, altered codon usage and controlling tRNA addition. Trapped LacY folding intermediates will be studied using biophysical methods.'

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