Mutation-tolerant protein identification by mass spectrometry.

J Comput Biol
Authors
Keywords
Abstract

Database search in tandem mass spectrometry is a powerful tool for protein identification. High-throughput spectral acquisition raises the problem of dealing with genetic variation and peptide modifications within a population of related proteins. A method that cross-correlates and clusters related spectra in large collections of uncharacterized spectra (i.e., from normal and diseased individuals) would be very valuable in functional proteomics. This problem is far from being simple since very similar peptides may have very different spectra. We introduce a new notion of spectral similarity that allows one to identify related spectra even if the corresponding peptides have multiple modifications/mutations. Based on this notion, we developed a new algorithm for mutation-tolerant database search as well as a method for cross-correlating related uncharacterized spectra.

Year of Publication
2000
Journal
J Comput Biol
Volume
7
Issue
6
Pages
777-87
Date Published
2000
ISSN
1066-5277
DOI
10.1089/10665270050514927
PubMed ID
11382361
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