Torna ai risultati della ricercaBando per assegno di ricerca
| Titolo del progetto di ricerca in italiano | Identificazione della relazione struttura-funzione nel meccanismo di dissipazione fotoprotettiva di LHCII |
|---|---|
| Titolo del progetto di ricerca in inglese | Identification of the structural/functional basis for photoprotective energy dissipation in LHCII |
| Area CUN | 05 - Scienze biologiche |
| S.S.D | BIO/04 - FISIOLOGIA VEGETALE |
| Descrizione sintetica in italiano | In order to identify the protein domains and chromophores involved in quenching, she/he will create a library of mutant strains that each express the Lhcb1 protein and lack one of the 14 Chls bound to each monomer. The quenching of singlet chlorophyll excited states, is not the only photoprotection mechanism at work. Chlorophyll triplet formation will also be determined on purified proteins by transient absorption (TA) in the ms range. In order to maintain the “native” folding of pigment-proteins, these will be purified from thylakoids and included in nanodiscs, a preparation which, unlike liposomes, minimises scattering and allows for ultrafast TA measurements. By including WT or mutant LHCs in nanodiscs, together with pH-sensor subunit PsbS, she/he will attempt to identify the physical mechanism and species involved in quenching reactions, triggered by lumenal acidification. |
| Descrizione sintetica in inglese | In order to identify the protein domains and chromophores involved in quenching, she/he will create a library of mutant strains that each express the Lhcb1 protein and lack one of the 14 Chls bound to each monomer. The quenching of singlet chlorophyll excited states, is not the only photoprotection mechanism at work. Chlorophyll triplet formation will also be determined on purified proteins by transient absorption (TA) in the ms range. In order to maintain the “native” folding of pigment-proteins, these will be purified from thylakoids and included in nanodiscs, a preparation which, unlike liposomes, minimises scattering and allows for ultrafast TA measurements. By including WT or mutant LHCs in nanodiscs, together with pH-sensor subunit PsbS, she/he will attempt to identify the physical mechanism and species involved in quenching reactions, triggered by lumenal acidification. |
| Data del bando | 27/09/2022 |
| Numero di assegnazioni per anno | 1 |
| Stanziamento annuale (indicativo) | 23900 |
| E' richiesta mobilità internazionale? | no |
| Paesi in cui può essere condotta la ricerca |
Italy |
| Paesi di residenza dei candidati |
OCEANIA NORTH AMERICA SOUTH AMERICA ASIA AFRICA EUROPE |
| Nazionalità dei candidati |
OCEANIA NORTH AMERICA SOUTH AMERICA ASIA AFRICA EUROPE |
| Sito web del bando | https://www.univr.it/it/concorsi/assegnisti-di-ricerca/assegni-di-ricerca/0/10661 |
| Destinatari dell'assegno di ricerca (of target group) |
Early stage researcher or 0-4 yrs (Post graduate) |
|---|---|
| Il contratto prevede la copertura delle prestazioni sociali? | yes |
| Importo annuale | 19367 |
| Valuta | Euro |
| Comprende lo stipendio dell'assegnista | yes |
| Comprende vitto e spese di viaggio | no |
| Comprende il costo della ricerca | no |
| Massima durata dell'assegno (mesi) | 24 |
| Criteri di selezione in italiano (breve descrizione) | In order to identify the protein domains and chromophores involved in quenching, she/he will create a library of mutant strains that each express the Lhcb1 protein and lack one of the 14 Chls bound to each monomer. The quenching of singlet chlorophyll excited states, is not the only photoprotection mechanism at work. Chlorophyll triplet formation will also be determined on purified proteins by transient absorption (TA) in the ms range. In order to maintain the “native” folding of pigment-proteins, these will be purified from thylakoids and included in nanodiscs, a preparation which, unlike liposomes, minimises scattering and allows for ultrafast TA measurements. By including WT or mutant LHCs in nanodiscs, together with pH-sensor subunit PsbS, she/he will attempt to identify the physical mechanism and species involved in quenching reactions, triggered by lumenal acidification. |
| Criteri di selezione in inglese (breve descrizione) | In order to identify the protein domains and chromophores involved in quenching, she/he will create a library of mutant strains that each express the Lhcb1 protein and lack one of the 14 Chls bound to each monomer. The quenching of singlet chlorophyll excited states, is not the only photoprotection mechanism at work. Chlorophyll triplet formation will also be determined on purified proteins by transient absorption (TA) in the ms range. In order to maintain the “native” folding of pigment-proteins, these will be purified from thylakoids and included in nanodiscs, a preparation which, unlike liposomes, minimises scattering and allows for ultrafast TA measurements. By including WT or mutant LHCs in nanodiscs, together with pH-sensor subunit PsbS, she/he will attempt to identify the physical mechanism and species involved in quenching reactions, triggered by lumenal acidification. |
| Processo di selezione in italiano (breve descrizione) | La selezione avverrà attraverso la valutazione dei titoli prodotti dai candidati e un colloquio. |
| Processo di selezione in inglese (breve descrizione) | The competition will be carried out by an evaluation of titles and examination by means of an interview. |
| Nome dell'Ente finanziatore | Università degli Studi di Verona - Dipartimento di Biotecnologie |
|---|---|
| Tipologia dell'Ente | Academic |
| Paese dell'Ente | Italy |
| Città | Verona |
| Codice postale | 37129 |
| Indirizzo | Via dell'Artigliere, 8 |
| Sito web | https://www.univr.it/home |
| elena.cordioli@univr.it | |
| Telefono | +39 (0)458028204 |
| L'assegno finanziato/cofinanziato attraverso un EU Research Framework Programme? | H2020/Erc |
|---|
| Data di scadenza del bando | 17/10/2022 |
|---|---|
| Come candidarsi | ufficio.protocollo@pec.univr.it |