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.

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

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.)

NPsVLCD (2019)

Natural Product-Inspired Therapies for Leishmaniasis and Chagas Disease

Read More  

NaWaTL (2020)

Narrative, Writing, and the Teotihuacan Language: Exploring Language History Through Phylogenetics, Epigraphy and Iconography

Read More  

Long-term migration (2019)

Immigration, Attitudes of Natives and Immigrants Assimilation

Read More