Signal Traitment and Virtual Images Production (2/2) View Full Text


Ontology type: schema:Chapter     


Chapter Info

DATE

2005-01-01

AUTHORS

M Muller , R Gras , R D Appel , W V Bienvenut , D F Hochstrasser

ABSTRACT

The molecular scanner combines protein separation using gel electrophoresis with peptide mass fingerprinting (PMF) techniques to identify proteins in a highly automated manner. Proteins separated in a 2-dimensional polyacrylamide gel (2D-PAGE) are digested ‘in parallel’ and transferred onto a membrane keeping their relative positions. The membrane is then sprayed with a matrix and inserted into a matrix-assisted laser desorption/ionization time-of-flight (MALDI-TOF) mass spectrometer, which measures a peptide mass fingerprint at each site on the scanned grid. First, visualization of PMF data allows surveying all fingerprints at once and provides very useful information on the presence of chemical noise. Chemical noise is shown to be a potential source for erroneous identifications and is therefore purged from the mass fingerprints. Then, the correlation between neighboring spectra is used to recalibrate the peptide masses. Finally, a method that clusters peptide masses according to the similarity of the spatial distributions of their signal intensities is presented. This method allows discarding many of the false positives that usually go along with PMF identifications and allows identifying many weakly expressed proteins present in the gel. More... »

PAGES

169-188

Book

TITLE

Acceleration and Improvement of Protein Identification by Mass Spectrometry

ISBN

978-1-4020-3318-6
978-1-4020-3319-3

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/1-4020-3319-2_5

DOI

http://dx.doi.org/10.1007/1-4020-3319-2_5

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1014090741


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