Utility of CE-MS data in protein identification. Academic Article

abstract

• A new method for displaying CE-MALDI-MS data for proteolytic digests is described. This data display mode yields distinct charge-based trends for plots of mass-to-charge (m/z) versus CE migration time. These trends arise owing to the in-solution charge state of the peptides, and this interpretation was confirmed by using empirical peptide electromigration models and peptide standards as charge-state markers. These charge-state specific trends exhibit analytical utility by providing additional chemical information about the peptides, which increases the confidence level of peptide identification and provides a rapid means for screening for posttranslationally modified peptides.

authors

• Russell, David

published proceedings

• Anal Chem

altmetric score

• 3

author list (cited authors)

• Williams, B. J., Russell, W. K., & Russell, D. H.

citation count

• 21

complete list of authors

• Williams, Brad J||Russell, William K||Russell, David H

publication date

• May 2007

publisher

• American Chemical Society (ACS)  Publisher

published in

• Analytical Chemistry  Journal

keywords

• Electrophoresis, Capillary
• Ions
• Protein Processing, Post-Translational
• Proteins
• Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization

PubMed Central ID

• 17411015

Digital Object Identifier (DOI)

• 10.1021/ac062395w

start page

• 3850

end page

• 3855

volume

• 79

issue

• 10

URL

• http://dx.doi.org/10.1021/ac062395w