FAPRMOL

Flow-aligned polarised Raman of biomacromolecular entities

 Coordinatore THE UNIVERSITY OF WARWICK 

 Organization address address: Kirby Corner Road - University House -
city: COVENTRY
postcode: CV4 8UW

contact info
Titolo: Dr.
Nome: Peter
Cognome: Hedges
Email: send email
Telefono: +44 24 7652 3716
Fax: +44 24 7652 4991

 Nazionalità Coordinatore United Kingdom [UK]
 Totale costo 0 €
 EC contributo 181˙350 €
 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) 2009-05-26   -   2011-05-25

 Partecipanti

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

 Organization address address: Kirby Corner Road - University House -
city: COVENTRY
postcode: CV4 8UW

contact info
Titolo: Dr.
Nome: Peter
Cognome: Hedges
Email: send email
Telefono: +44 24 7652 3716
Fax: +44 24 7652 4991

UK (COVENTRY) coordinator 181˙350.77

Mappa


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fapr    membrane    radiation    environments    uv    proteins    data    structure    interactions   

 Obiettivo del progetto (Objective)

'Existing spectroscopic methods do not provide satisfactory data on structure, orientation and interactions of biomacromolecules in their native environments. This is especially true of membrane proteins, a major class of drug target. The structure of formulated glycoprotein biopharmaceuticals and their interactions with their targets are also a challenge for UV spectroscopies due to extremely high concentrations and the near invisibility of the sugars to UV radiation. Infra red methods suffer from water absorbance dominating the analyte signals. We will therefore develop a new technique called flow-aligned polarised Raman (FAPR) spectroscopy, which will have many of the advantages of existing techniques, including using aqueous environments, while avoiding their pitfalls by using visible radiation. We expect to gain new structural data on the studied molecules using FAPR. The applicability of this method will be verified on membrane peptides and proteins and glycoproteins.'

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