Imperial College London
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ProfessorVitaliAverbukh

Faculty of Natural Sciences, Department of Physics

Professor of Molecular Physics
 
 
 
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Contact

 

+44 (0)20 7594 7746v.averbukh Website

 
 
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Location

 

209Blackett LaboratorySouth Kensington Campus

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Summary

 

Publications

Citation

BibTex format

@unpublished{Driver:2019,
author = {Driver, T and Ayers, R and Pipkorn, R and Cooper, B and Bachhawat, N and Patchkovskii, S and Averbukh, V and Klug, DR and Marangos, JP and Frasinski, LJ and Edelson-Averbukh, M},
title = {Partial covariance two-dimensional mass spectrometry for determination  of biomolecular primary structure},
url = {http://arxiv.org/abs/1904.05946v1},
year = {2019}
}
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RIS format (EndNote, RefMan)

TY  - UNPB
AB  - Mass spectrometry (MS) is used widely in biomolecular structural analysis andis particularly dominant in the study of proteins. Despite its considerablepower, state-of-the-art protein MS frequently suffers from limited reliabilityof spectrum-to-structure assignments. This could not be solved fully by thedramatic increase in mass accuracy and resolution of modern MS instrumentationor by the introduction of new fragmentation methods. Here we present a new kindof two-dimensional mass spectrometry for high fidelity determination of abiomolecular primary structure based on partial covariance mapping. Partialcovariance two-dimensional mass spectrometry (pC-2DMS) detects intrinsicstatistical correlations between biomolecular fragments originating from thesame or consecutive decomposition events. This enables identification of pairsof ions produced along the same fragmentation pathway of a biomolecule acrossits entire fragment mass spectrum. We demonstrate that the fragment-fragmentcorrelations revealed by pC-2DMS provide much more specific information on theamino acid sequence and its covalent modifications than the individual fragmentmass-to-charge ratios on which standard one-dimensional MS is based. Weillustrate the power of pC-2DMS by using it to resolve structural isomers ofcombinatorially modified histone peptides inaccessible to standard MS.
AU  - Driver,T
AU  - Ayers,R
AU  - Pipkorn,R
AU  - Cooper,B
AU  - Bachhawat,N
AU  - Patchkovskii,S
AU  - Averbukh,V
AU  - Klug,DR
AU  - Marangos,JP
AU  - Frasinski,LJ
AU  - Edelson-Averbukh,M
PY  - 2019///
TI  - Partial covariance two-dimensional mass spectrometry for determination  of biomolecular primary structure
UR  - http://arxiv.org/abs/1904.05946v1
ER  -
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