NDLI: Protein identification using sequential ion/ion reactions and tandem mass spectrometry

Content Provider	PubMed Central
Author	Coon, Joshua J. Beatrix, Ueberheide Syka, John E. P. Dryhurst, Deanna D. Ausio, Juan Jeffrey, Shabanowitz Hunt, Donald F.
Copyright Year	2005
Abstract	A method for rapid sequencing of intact proteins simultaneously from the N and C termini (1–2 s) with online chromatography is described and applied to the characterization of histone H3.1 posttranslational modifications and the identification of an additional member of the H2A gene family. Proteins are converted to gas-phase multiply charged positive ions by electrospray ionization and then allowed to react with fluoranthene radical anions. Electron transfer to the multiply charged protein promotes random dissociation of the N—Cα bonds of the protein backbone. Multiply charged fragment ions are then deprotonated in a second ion/ion reaction with the carboxylate anion of benzoic acid. The m/z values for the resulting singly and doubly charged ions are used to read a sequence of 15–40 aa at both the N and C termini of the protein. This information, with the measured mass of the intact protein, is used to search protein or nucleotide databases for possible matches, detect posttranslational modifications, and determine possible splice variants.
Related Links	http://dx.doi.org/10.1073/pnas.0503189102
Ending Page	9468
Page Count	6
Starting Page	9463
File Format	PDF
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	27
Volume Number	102
Language	English
Publisher	National Academy of Sciences
Publisher Date	2005-07-05
Access Restriction	Open
Rights Holder	National Academy of Sciences
Subject Keyword	General Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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