Imperial College London
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Professor LESZEK Frasinski

Faculty of Natural Sciences, Department of Physics

Professor in Atomic and Molecular Physics
 
 
 
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Contact

 

l.j.frasinski CV

 
 
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Assistant

 

Ms Judith Baylis +44 (0)20 7594 7713

 
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Location

 

206Blackett LaboratorySouth Kensington Campus

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Summary

 

Publications

Citation

BibTex format

@article{Driver:2021:10.1021/acs.analchem.1c00332,
author = {Driver, T and Averbukh, V and Frasiski, LJ and Marangos, JP and Edelson-Averbukh, M},
doi = {10.1021/acs.analchem.1c00332},
journal = {Analytical Chemistry},
pages = {10779--10788},
title = {Two-dimensional partial covariance mass spectrometry for the top-down analysis of intact proteins.},
url = {http://dx.doi.org/10.1021/acs.analchem.1c00332},
volume = {93},
year = {2021}
}
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RIS format (EndNote, RefMan)

TY  - JOUR
AB  - Two-dimensional partial covariance mass spectrometry (2D-PC-MS) exploits the inherent fluctuations of fragment ion abundances across a series of tandem mass spectra, to identify correlated pairs of fragment ions produced along the same fragmentation pathway of the same parent (e.g., peptide) ion. Here, we apply 2D-PC-MS to the analysis of intact protein ions in a standard linear ion trap mass analyzer, using the fact that the fragment-fragment correlation signals are much more specific to the biomolecular sequence than one-dimensional (1D) tandem mass spectrometry (MS/MS) signals at the same mass accuracy and resolution. We show that from the distribution of signals on a 2D-PC-MS map it is possible to extract the charge state of both parent and fragment ions without resolving the isotopic envelope. Furthermore, the 2D map of fragment-fragment correlations naturally separates the products of the primary decomposition pathways of the molecular ions from those of the secondary ones. We access this spectral information using an adapted version of the Hough transform. We demonstrate the successful identification of highly charged, intact protein molecules bypassing the need for high mass resolution. Using this technique, we also perform the in silico deconvolution of the overlapping fragment ion signals from two co-isolated and co-fragmented intact proteins, demonstrating a viable new method for the concurrent mass spectrometric identification of a mixture of intact protein ions from the same fragment ion spectrum.
AU  - Driver,T
AU  - Averbukh,V
AU  - Frasiski,LJ
AU  - Marangos,JP
AU  - Edelson-Averbukh,M
DO  - 10.1021/acs.analchem.1c00332
EP  - 10788
PY  - 2021///
SN  - 0003-2700
SP  - 10779
TI  - Two-dimensional partial covariance mass spectrometry for the top-down analysis of intact proteins.
T2  - Analytical Chemistry
UR  - http://dx.doi.org/10.1021/acs.analchem.1c00332
UR  - https://www.ncbi.nlm.nih.gov/pubmed/34309360
UR  - https://pubs.acs.org/doi/10.1021/acs.analchem.1c00332https://pubs.acs.org/doi/10.1021/acs.analchem.1c00332
UR  - http://hdl.handle.net/10044/1/90619
VL  - 93
ER  -
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