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PHOTO_IMS

The use of mass spectrometry and optical methods to determine the influence of cofactors on the structure and stability of proteins

Total Cost €

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EC-Contrib. €

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Project "PHOTO_IMS" data sheet

The following table provides information about the project.

Coordinator
THE UNIVERSITY OF MANCHESTER 

Organization address
address: OXFORD ROAD
city: MANCHESTER
postcode: M13 9PL
website: www.manchester.ac.uk

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]
 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-2016
 Funding Scheme MSCA-IF-EF-ST
 Starting year 2018
 Duration (year-month-day) from 2018-03-01   to  2020-02-29

 Partnership

Take a look of project's partnership.

# participants  country  role  EC contrib. [€] 
1    THE UNIVERSITY OF MANCHESTER UK (MANCHESTER) coordinator 195˙454.00

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 Project objective

This fellowship will use novel instrumentation to define the role of cofactors on the structure and stability of proteins. We have recently adapted a commercially available Synapt ion mobility mass spectrometer to allow it to perform optical measurements on conformer and mass selected ions, in collaboration with Waters Corp. The heart of this instrument is the ion mobility cell, IM-MS measurements are possible in this instrument, as for any Synapt mass spectrometer, but uniquely we are able to trap ions that have been conformer selected, to allow optical measurements in a so called ‘photo SRIG’ (stacked ring ion guide). Such optical measurements can take several forms, including IR-spectroscopy, UV/Vis-spectroscopy, which will provide structural analysis of co-factors and coenzymes, photo-dissociation to sequence the proteins as well as fluorescence to probe global conformations. Molecular mechanics calculations will generate structures to compare with those determined experimentally. This MC fellow will use this novel instrument to examine the role of cofactors on the conformations of proteins, by making measurements on the cofactor alone, the apo and the holo form of the protein. The MC fellow will be trained in biological mass spectrometry, in optical methods and in molecular mechanics. They will spend a secondment at Waters developing software to best interpret the data from this instrument. This cutting edge interdisciplinary science program is world leading and will train this fellow with a set of skills highly desirable both in academia and in industry.

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

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