Opendata, web and dolomites

OCPSTRUCTDYNAMICS SIGNED

Structural dynamics essential for photosynthetic adaptation and survival of cyanobacteria in fluctuating light intensities

Total Cost €

0

EC-Contrib. €

0

Partnership

0

Views

0

 OCPSTRUCTDYNAMICS project word cloud

Explore the words cloud of the OCPSTRUCTDYNAMICS project. It provides you a very rough idea of what is the project "OCPSTRUCTDYNAMICS" about.

transitions    photoprotective    heat    terminal    biofuel    photosynthetic    domains    spectroscopic    spectroscopy    photoactivation    gene    ultrafast    cyanobacterial    photo    excess    ray    protein    resolved    transient    polarised    dissociation    time    energy    suggested    dependent    machinery    additional    protect    absorbed    proteins    intensity    identification    carotenoid    crystallography    roles    kinetics    orange    genomes    dynamics    date    single    damage    npq    mechanism    photosynthesis    structural    describe    triggered    mechanisms    isolated    photochemical    structure    6803    harvesting    slr1963    demonstrating    movement    themselves    combined    fluctuations    encoded    dissipation    artificial    exact    allowed    crystals    ocp1    ocpx    like    absorption    resolve    subfamilies    paralogs    photoprotection    raised    light    organisms    causing    oriented    occurs    photoenergy    performed    cyanobacteria    diffraction    ocp2    flow    questions    ranging    optogenetics    synechocystis    first    ocp    vulnerable    differences    unravelled    activation    quenching    interactions   

Project "OCPSTRUCTDYNAMICS" data sheet

The following table provides information about the project.

Coordinator
IMPERIAL COLLEGE OF SCIENCE TECHNOLOGY AND MEDICINE 

Organization address
address: SOUTH KENSINGTON CAMPUS EXHIBITION ROAD
city: LONDON
postcode: SW7 2AZ
website: http://www.imperial.ac.uk/

contact info
title: n.a.
name: n.a.
surname: n.a.
function: n.a.
email: n.a.
telephone: n.a.
fax: n.a.

 Coordinator Country United Kingdom [UK]
 Total cost 212˙933 €
 EC max contribution 212˙933 € (100%)
 Programme 1. H2020-EU.1.3.2. (Nurturing excellence by means of cross-border and cross-sector mobility)
 Code Call H2020-MSCA-IF-2018
 Funding Scheme MSCA-IF-EF-ST
 Starting year 2020
 Duration (year-month-day) from 2020-01-08   to  2022-01-07

 Partnership

Take a look of project's partnership.

# participants  country  role  EC contrib. [€] 
1    IMPERIAL COLLEGE OF SCIENCE TECHNOLOGY AND MEDICINE UK (LONDON) coordinator 212˙933.00

Map

 Project objective

Like most photosynthetic organisms, cyanobacteria are vulnerable to fluctuations in light intensity, which can damage their photosynthetic machinery. To protect themselves against such fluctuations, they use a photoprotective mechanism called non-photochemical quenching (NPQ), i.e. the dissipation of excess absorbed photo-energy as heat. NPQ in cyanobacteria is triggered by orange carotenoid protein (OCP) light activation. Based on spectroscopic and diffraction studies of OCP in Synechocystis 6803 (gene slr1963), it was suggested that OCP light activation occurs through light-induced movement of a carotenoid causing movement and/or dissociation of OCP N- and C-terminal domains. However, the exact structural dynamics of OCP light-activation need to be unravelled. Furthermore, the growing availability of cyanobacterial genomes allowed identification of additional OCP subfamilies (OCP2, OCPX) in different cyanobacteria. The first results demonstrating different kinetics of light-activation in the different OCP paralogs raised questions about differences in their photoprotective roles and in photoactivation mechanisms. This topic has not been studied to date. Here I propose to resolve structural changes during photoprotection-related transitions of OCP in different OCP subfamilies using time-resolved X-ray crystallography. X-ray crystallography of OCP1 encoded by slr1963, the best-characterized OCP protein, as well as its paralogs from the OCP2 and OCPX subfamilies will be performed. This approach will be combined with ultrafast transient (polarised) absorption spectroscopy on isolated proteins and oriented single crystals to describe the structure-dependent flow of photoenergy in the proteins. This study has several potential applications ranging from enhancing cyanobacterial light harvesting to improve biofuel production, to better understanding of carotenoid-protein interactions in artificial photosynthesis systems, and for optogenetics.

Are you the coordinator (or a participant) of this project? Plaese send me more information about the "OCPSTRUCTDYNAMICS" project.

For instance: the website url (it has not provided by EU-opendata yet), the logo, a more detailed description of the project (in plain text as a rtf file or a word file), some pictures (as picture files, not embedded into any word file), twitter account, linkedin page, etc.

Send me an  email (fabio@fabiodisconzi.com) and I put them in your project's page as son as possible.

Thanks. And then put a link of this page into your project's website.

The information about "OCPSTRUCTDYNAMICS" are provided by the European Opendata Portal: CORDIS opendata.

More projects from the same programme (H2020-EU.1.3.2.)

COSMOS (2020)

The Conformation Of S-phase chroMOSomes

Read More  

GENESIS (2020)

unveilinG cEll-cell fusioN mEdiated by fuSexins In chordateS

Read More  

BIOplasma (2019)

Use flexible Tube Micro Plasma (FµTP) for Lipidomics

Read More