CONFBIO
Conformations and Interactions of Biologically Relevant Molecules
| Coordinatore | KING'S COLLEGE LONDON
Organization address
address: Strand contact info |
| Nazionalità Coordinatore | United Kingdom [UK] |
| Totale costo | 100˙000 € |
| EC contributo | 100˙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-2012-CIG |
| Funding Scheme | MC-CIG |
| Anno di inizio | 2013 |
| Periodo (anno-mese-giorno) | 2013-05-01 - 2017-04-30 |
Partecipanti
| # | ||||
|---|---|---|---|---|
| 1 |
KING'S COLLEGE LONDON
Organization address
address: Strand contact info |
UK (LONDON) | coordinator | 100˙000.00 |
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Obiettivo del progetto (Objective)
'Biological processes like molecular recognition, membrane transport, and folding and unfolding of proteins occur when the molecules involved have appropriate structures and interact in a specific way. However, a detailed knowledge of the structures of biologically-relevant molecules and the forces that give rise to them is still lacking for many processes. The aim of this project is to determine the structures of biologically relevant molecules and their interactions. We will examine the conformational space of several chiral odorants to explore the possible link between conformational flexibility and enantiomeric discrimination of odorants. We will study carvone, nootkatone and methyl-gamma-cyclogeranate, with enantiomers that smell differently, and fenchone, gamma-octathionolactone and tetrahydronootkatone, with enantiomers that smell the same. Interactions between these odorants and receptors in the ligand-binding site will be modeled by studying complexes formed between odorants and mimics of amino acid residues. The results will help gain insight into the molecular mechanisms of olfaction. We will also study changes induced by post-translational modifications, specifically glycosylation, phosphorylation and acetylation. Post-translational modifications of proteins that alter amino acid side chains exert a great influence in overall protein conformation, function, stability and dynamics. We will investigate the conformational landscape of several modified amino acids to determine their preferred structures and the relevant intramolecular forces that stabilise them. The results will yield new experimental data of immediate use for the bioinformatics community. To conduct this research a novel instrument combining broadband rotational spectroscopy with heating and laser ablation will be built. This instrument will be an invaluable resource for structural studies that will outlast the duration of this research project'