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HelixMold SIGNED

Computational design of novel functions in helical proteins by deviating from ideal geometries

Total Cost €

0

EC-Contrib. €

0

Partnership

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 HelixMold project word cloud

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

idealized    rationally    unsolved    specified    interdisciplinary    designed    ensembles    harsh    binding    helix    bind    stable    geometries    relying    envisioned    biophysical    protein    coil    first    extraordinary    tolerance    genetically    catalytically    bundle    crystallographic    harness    larger    experimental    harnessing    isolate    stability    revolutionize    repeating    structure    backbones    crick    site    heptad    classic    usually    sequence    computationally    functionalization    robustly    strategies    reactions    helical    proteins    coiled    made    followed    space    environments    chemical    geometry    parametric    encodable    regions    ligand    progress    constraints    tremendous    active    desired    mutagenesis    thermodynamic    functional    de    introduce    function    parametrically    biotechnological    deviations    code    critical    remediation    bundles    solvents    novo    accounting    glyphosate    saturation    expands    designs    nature    thermostability    ideal    units    resistance    computational    parametrization    follow    biomedical    model    strategy    organic    sites    cascade   

Project "HelixMold" data sheet

The following table provides information about the project.

Coordinator
TECHNISCHE UNIVERSITAET GRAZ 

Organization address
address: RECHBAUERSTRASSE 12
city: GRAZ
postcode: 8010
website: www.tugraz.at

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 Austria [AT]
 Total cost 1˙499˙414 €
 EC max contribution 1˙499˙414 € (100%)
 Programme 1. H2020-EU.1.1. (EXCELLENT SCIENCE - European Research Council (ERC))
 Code Call ERC-2018-STG
 Funding Scheme ERC-STG
 Starting year 2019
 Duration (year-month-day) from 2019-04-01   to  2024-03-31

 Partnership

Take a look of project's partnership.

# participants  country  role  EC contrib. [€] 
1    TECHNISCHE UNIVERSITAET GRAZ AT (GRAZ) coordinator 1˙499˙414.00

Map

 Project objective

We propose to computationally design novel ligand binding and catalytically active proteins by harnessing the high thermodynamic stability of de novo helical proteins. Tremendous progress has been made in protein design. However, the ability to robustly introduce function into genetically encodable de novo proteins is an unsolved problem. We will follow a highly interdisciplinary computational-experimental approach to address this challenge and aim to: -Characterize to which extent we can harness the stability of parametrically designed helical bundles to introduce deviations from ideal geometry. Ensembles of idealized de novo helix bundle backbones will be generated using our established parametric design code and designed with constraints accounting for an envisioned functional site. This will be followed by detailed computational, biophysical, crystallographic and site-saturation mutagenesis analysis to isolate critical design features. -Develop a new computational design strategy, which expands on the Crick coiled-coil parametrization and allows to rationally build non-ideal helical protein backbones at specified regions in the desired structure. This will enable us to model backbones around binding/active sites. We will design sites to bind glyphosate, for which remediation is highly needed. By using non-ideal geometries and not relying on classic heptad repeating units, we will be able to access a much larger sequence to structure space than is usually available to nature, enabling us to build more specific and more stable binding/catalytically active proteins. -Investigate new strategies to design the first cascade reactions into de novo designs. This research will allow functionalization of de novo designed proteins with high thermostability, extraordinary resistance to harsh chemical environments and high tolerance for organic solvents and has the potential to revolutionize how proteins for biotechnological and biomedical applications are generated.

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

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