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Single Molecule Study of Protease Mechano-Specificity

Total Cost €


EC-Contrib. €






 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.

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Project "MECHANOPROTEASES" data sheet

The following table provides information about the project.


Organization address
address: STRAND
city: LONDON
postcode: WC2R 2LS

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]
 Project website
 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


Take a look of project's partnership.

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


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

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