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MECHANOPROTEASES

Single Molecule Study of Protease Mechano-Specificity

Total Cost €

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EC-Contrib. €

0

Partnership

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 MECHANOPROTEASES project word cloud

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

molecule    enzymology    anticipate    dissect    bound    proteases    single    ultimately    question    mechanisms    biochemistry    techniques    protease    structural    buried    kinetics    stretching    disulfide    mediated    chemical    elusive    favoring    occurs    highlight    spectroscopy    rate    experiments    discoveries    bioinformatics    substrate    permitting    tempting    discovered    implying    specificity    forces    innovative    assembly    relies    hence    geometry    force    inhibits    mechanobiology    unfolding    chemistry    enzymatic    proteolysis    curved    unapproachable    unanticipated    elucidate    dependent    probe    bond    clamp    reaction    molecular    reactions    subsequent    proteins    mechanical    offers    catalytic    vivo    biology    previously    unveil    decades    speculate    engineering    successful    mechano    newly    cryptic    effect    relation    possibilities    vastly    underlie    exponentially    technique    sites    nucleophile    close    understand    proteasome    degradation    hydrolysis    catalysis    protein    enzyme    bulk    multidisciplinary    character    series   

Project "MECHANOPROTEASES" data sheet

The following table provides information about the project.

Coordinator
KING'S COLLEGE LONDON 

Organization address
address: STRAND
city: LONDON
postcode: WC2R 2LS
website: www.kcl.ac.uk

contact info
title: n.a.
name: n.a.
surname: n.a.
function: n.a.
email: n.a.
telephone: n.a.
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 Coordinator Country United Kingdom [UK]
 Project website https://www.kcl.ac.uk/
 Total cost 195˙454 €
 EC max contribution 195˙454 € (100%)
 Programme 1. H2020-EU.1.3.2. (Nurturing excellence by means of cross-border and cross-sector mobility)
 Code Call H2020-MSCA-IF-2014
 Funding Scheme MSCA-IF-EF-ST
 Starting year 2015
 Duration (year-month-day) from 2015-04-01   to  2017-03-31

 Partnership

Take a look of project's partnership.

# participants  country  role  EC contrib. [€] 
1    KING'S COLLEGE LONDON UK (LONDON) coordinator 195˙454.00

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 Project objective

Single-molecule enzymology offers new possibilities to dissect catalytic reactions that were previously unapproachable using biochemistry techniques conducted in the bulk. In particular, recent discoveries conducted at the single molecule level, such as the unanticipated force-mediated protein degradation pathway in the proteasome, highlight the close relation between mechanical forces and proteolysis in vivo. While much has been discovered about protein enzymology in the recent decades, the question of how mechanical force affects enzymatic catalysis remains vastly elusive. The main goal of this proposal is to understand the mechanobiology of proteolysis at the single molecule level. We will use the newly developed force-clamp spectroscopy technique, together with molecular biology engineering techniques and bioinformatics structural analysis to elucidate the molecular mechanisms that underlie protease catalysis under mechanical force. Successful enzymatic activity relies on the enzyme:substrate (E:S) assembly. Upon mechanical unfolding, proteins unveil their buried substrate sites, also called cryptic sites, thus favoring the formation of the E:S complex and ultimately permitting the subsequent chemical reaction. A key feature of recent mechano-chemistry experiments at the single bond level is that the rate at which the reduction of a protein disulfide bond occurs in the presence of a nucleophile is exponentially dependent on the stretching force. Hence, it is tempting to speculate that, in the case of an enzymatic reaction, the catalytic rate will be also force-dependent. We anticipate that the curved geometry of the bound substrate inhibits the E:S assembly at high-forces, implying a novel mechano-specificity character of proteases. Within a multidisciplinary approach, here we propose a series of innovative experiments to directly probe the effect of force on the kinetics of protease hydrolysis.

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