Explore the words cloud of the LIQUIDMASS project. It provides you a very rough idea of what is the project "LIQUIDMASS" about.
The following table provides information about the project.
Coordinator |
AGENCIA ESTATAL CONSEJO SUPERIOR DEINVESTIGACIONES CIENTIFICAS
Organization address contact info |
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 |
Take a look of project's partnership.
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1 | AGENCIA ESTATAL CONSEJO SUPERIOR DEINVESTIGACIONES CIENTIFICAS | ES (MADRID) | coordinator | 2˙470˙283.00 |
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.
year | authors and title | journal | last update |
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2019 |
Laura Zarraoa, MarÃa U. González, Ãlvaro 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, MarÃa U. González, Ãlvaro 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, Ãlvaro T. Omori, Edgard A. Ferreira, Denise F.S. Petri, Óscar Malvar, Carmen M. DomÃnguez, 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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