PHOTORECEPTION

Photoactive proteins: from the intrinsic properties of biochromophores towards the ultra-fast excited-state reaction dynamics in photoreceptors

 Coordinatore AARHUS UNIVERSITET 

 Organization address address: Nordre Ringgade 1
city: AARHUS C
postcode: 8000

contact info
Titolo: Ms.
Nome: Bodil
Cognome: Mølgaard
Email: send email
Telefono: +45 8942 3582

 Nazionalità Coordinatore Denmark [DK]
 Totale costo 50˙000 €
 EC contributo 50˙000 €
 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-2011-CIG
 Funding Scheme MC-CIG
 Anno di inizio 2011
 Periodo (anno-mese-giorno) 2011-09-01   -   2013-08-31

 Partecipanti

# participant  country  role  EC contrib. [€] 
1    AARHUS UNIVERSITET

 Organization address address: Nordre Ringgade 1
city: AARHUS C
postcode: 8000

contact info
Titolo: Ms.
Nome: Bodil
Cognome: Mølgaard
Email: send email
Telefono: +45 8942 3582

DK (AARHUS C) coordinator 50˙000.00

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chromophore    wavelength    proteins    excited    biological    photoreceptors    interactions    atomic    dynamics    vision    photoactive    studying    quantum    hosting   

 Obiettivo del progetto (Objective)

'The project is aimed at studying photoactive proteins at the atomic level theoretically as well as experimentally. Photoactive proteins are widespread in nature and enable the signal transduction in biological photoreceptors triggered by the absorption of a photon with a particular wavelength. Opsin proteins containing a protonated Schiff-base retinal chromophore are perhaps the best known as they provide vision in vertebrates.

We will study the photophysical and photochemical properties of the chromophores of these proteins at different levels: intrinsic properties of the isolated chromophore units, then the well-defined atomic-scale interactions with the hosting protein medium in the binding site of the chromophore, and finally, whole proteins. One of the highlight goals is to understand the catalytic role played by proteins in the ultrafast excited-state reaction dynamics of biological photoreceptors and in the self-regulation of their photo-physical properties at the atomic-scale. Ultimately, this will lead to an understanding of both wavelength tuning and efficiency of the primary photoreaction in the vision process.

Our strategy is to combine the expertise of the applicant in the field of the state-of-the-art quantum methods, who is a co-developer of one of the leading quantum chemistry packages, with the leadership of the hosting university when it comes to laser-action spectroscopy techniques for studying the biomolecular ions in the gas phase. We believe, that such collaboration forms a firm ground for the joint project with the mutual benefit of supporting experimental findings by theory and achieving a better understanding of the underlying fundamental atomic-scale interactions and excited-state dynamics in photoactive biosystems.'

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