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

Summary
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.
Unfold all
/
Fold all
More information & hyperlinks
Web resources: https://cordis.europa.eu/project/id/750642
Start date: 01-03-2018
End date: 29-02-2020
Total budget - Public funding: 195 454,80 Euro - 195 454,00 Euro
Cordis data

Original description

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.

Status

CLOSED

Call topic

MSCA-IF-2016

Update Date

28-04-2024
Images
No images available.
Geographical location(s)
Structured mapping
Unfold all
/
Fold all
Horizon 2020
H2020-EU.1. EXCELLENT SCIENCE
H2020-EU.1.3. EXCELLENT SCIENCE - Marie Skłodowska-Curie Actions (MSCA)
H2020-EU.1.3.2. Nurturing excellence by means of cross-border and cross-sector mobility
H2020-MSCA-IF-2016
MSCA-IF-2016