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LIQUIDMASS SIGNED

High throughput mass spectrometry of single proteins in liquid environment

Total Cost €

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EC-Contrib. €

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Partnership

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Project "LIQUIDMASS" data sheet

The following table provides information about the project.

Coordinator
AGENCIA ESTATAL CONSEJO SUPERIOR DEINVESTIGACIONES CIENTIFICAS 

Organization address
address: CALLE SERRANO 117
city: MADRID
postcode: 28006
website: http://www.csic.es

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 Spain [ES]
 Project website https://ercliquidmass.eu
 Total cost 2˙470˙283 €
 EC max contribution 2˙470˙283 € (100%)
 Programme 1. H2020-EU.1.1. (EXCELLENT SCIENCE - European Research Council (ERC))
 Code Call ERC-2015-CoG
 Funding Scheme ERC-COG
 Starting year 2016
 Duration (year-month-day) from 2016-11-01   to  2021-10-31

 Partnership

Take a look of project's partnership.

# participants  country  role  EC contrib. [€] 
1    AGENCIA ESTATAL CONSEJO SUPERIOR DEINVESTIGACIONES CIENTIFICAS ES (MADRID) coordinator 2˙470˙283.00

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 Project objective

Although mass spectrometry has brought about major advancements in proteomics in the last decade, protein mass spectrometers still have important limitations. One fundamental limitation is that they require sample ionization, desorption into the gas phase and fragmentation, clearly leading to protein denaturation. Since relevant protein complexes are unstable or transient, their characterization in its native state and physiological environment remains an unexplored route towards the full understanding of protein function and protein interactions. This problem has only been targeted to date through theoretical approaches or low throughput experimental techniques, such as atomic force spectroscopy, optical tweezers or FRET. A high throughput characterization technology capable of addressing single proteins in its native state would have a large impact in proteomics. The goal of LIQUIDMASS is to develop a high throughput spectrometric technique addressing single proteins from complex samples while in physiological conditions. LIQUIDMASS also proposes a new concept for protein spectrometry, by characterizing not only the mass, but also the hydrodynamic radius, geometry and stiffness of single proteins. This multiparameter approach will serve to open up new routes to understand protein structure-function relations by providing insight into the fast conformational changes that occur in liquids. In order to attain these goals, I propose to integrate nanomechanical resonators, nano-optics and nanofluidics. The disruptive approach proposed will bring about new knowledge about protein interactions and protein conformation that is elusive today. The enabling technologies aimed at the LIQUIDMASS will increase our understanding of protein misfolding related diseases, such as Alzheimer’s or diabetes, as well as bring closer a full understanding of the human interactome, contributing to the advancement of the proteomics field.

 Publications

year authors and title journal last update
List of publications.
2019 Laura Zarraoa, María U. González, Álvaro San Paulo
Imaging low-dimensional nanostructures by very low voltage scanning electron microscopy: ultra-shallow topography and depth-tunable material contrast
published pages: , ISSN: 2045-2322, DOI: 10.1038/s41598-019-52690-9
Scientific Reports 9/1 2020-01-28
2019 Laura Zarraoa, María U. González, Álvaro San Paulo
Imaging low-dimensional nanostructures by very low voltage scanning electron microscopy: ultra-shallow topography and depth-tunable material contrast
published pages: , ISSN: 2045-2322, DOI: 10.1038/s41598-019-52690-9
Scientific Reports 9/1 2019-12-16
2018 Daniel Ramos, Oscar Malvar, Zachary J. Davis, Javier Tamayo, Montserrat Calleja
Nanomechanical Plasmon Spectroscopy of Single Gold Nanoparticles
published pages: 7165-7170, ISSN: 1530-6984, DOI: 10.1021/acs.nanolett.8b03236
Nano Letters 18/11 2019-08-29
2018 J. J. Ruz, V. Pini, O. Malvar, P. M. Kosaka, M. Calleja, J. Tamayo
Effect of surface stress induced curvature on the eigenfrequencies of microcantilever plates
published pages: 105213, ISSN: 2158-3226, DOI: 10.1063/1.5053561
AIP Advances 8/10 2019-05-13
2019 Roseli H. Sato, Priscila M. Kosaka, Álvaro T. Omori, Edgard A. Ferreira, Denise F.S. Petri, Óscar Malvar, Carmen M. Domínguez, Valerio Pini, Óscar Ahumada, Javier Tamayo, Montserrat Calleja, Rodrigo L.O.R. Cunha, Pablo A. Fiorito
Development of a methodology for reversible chemical modification of silicon surfaces with application in nanomechanical biosensors
published pages: 287-293, ISSN: 0956-5663, DOI: 10.1016/j.bios.2019.04.028
Biosensors and Bioelectronics 137 2019-08-29

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