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The Dynamic Composition of the Protein Chaperone Network: Unraveling Human Protein Disaggregation via NMR Spectroscopy

Total Cost €


EC-Contrib. €






 NMR-DisAgg project word cloud

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

aggregates    ultimately    disaggregation    chaperones    aside    break    methyl    initial    families    dissolving    molecular    monitor    series    course    first    biophysical    chaperone    responsible    trosy    performing    exact    suited    regarding    assays    observe    homeostasis    dnaj    recognition    hsp40    structure    amyloids    itself    neurodegenerative    client    structural    potentially    ideally    substrate    remodeling    characterization    dynamic    group    cest    proven    lab    apart    cpmg    nature    members    amyloid    hsp70    host    certain    critical    populated    experiments    reaction    perform    schemes    protein    techniques    diverse    types    clients    complexes    refolding    little    toxic    discovered    cellular    combining    recognizing    small    diseases    transient    labeling    protect    nmr    disease    cells    combinations    human    extremely    interactions    additional    linked    shock    proteins    fibers    though    performed    functional    time    functions    heat    operate    shsp    maintaining   

Project "NMR-DisAgg" data sheet

The following table provides information about the project.


Organization address
address: HERZL STREET 234
postcode: 7610001

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 Israel [IL]
 Total cost 1˙499˙956 €
 EC max contribution 1˙499˙956 € (100%)
 Programme 1. H2020-EU.1.1. (EXCELLENT SCIENCE - European Research Council (ERC))
 Code Call ERC-2018-STG
 Funding Scheme ERC-STG
 Starting year 2018
 Duration (year-month-day) from 2018-09-01   to  2023-08-31


Take a look of project's partnership.

# participants  country  role  EC contrib. [€] 
1    WEIZMANN INSTITUTE OF SCIENCE IL (REHOVOT) coordinator 1˙499˙956.00


 Project objective

Molecular chaperones are a diverse group of proteins critical to maintaining cellular homeostasis. Aside from protein refolding, it has recently been discovered that certain combinations of human chaperones can break apart toxic protein aggregates and even amyloids that have been linked to a host of neurodegenerative diseases. The first chaperones in this disaggregation reaction that are responsible for recognizing and performing initial remodeling of aggregates, are members of the Hsp40 (DnaJ) and small heat shock protein (sHSP) families. Very little, though, is known regarding how these chaperones perform their functions, and characterization of sHsp- and DnaJ-substrate complexes by most structural techniques has proven extremely challenging, as most chaperones are dynamic in nature and typically operate through a series of transient interactions with both their clients and other chaperones. The advanced NMR techniques used in our lab, however, are ideally suited for the study of these exact types of dynamic systems, and include recently developed experiments (CEST, CPMG) that allow us to monitor the transient and low populated protein states typical of chaperone-chaperone and chaperone-client interactions, as well as to study the structure of these potentially very large protein complexes (methyl-TROSY). By exploiting these NMR methodologies and additional, novel labeling schemes, we will characterize, for the first time, the recognition and substrate remodeling performed by the many members of the DnaJ and sHsp chaperone families on their clients. We will then take these approaches one step further and develop real time NMR experiments to observe the client remodeling performed over the course of the disaggregation reaction itself. By combining advanced NMR with biophysical and functional assays, we ultimately aim to identify the specific sets of chaperones that, with the Hsp70 system, protect our cells by dissolving disease-linked aggregates and amyloid fibers.

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