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Retention time prediction and protein identification

Palmblad, M. (2007) Retention time prediction and protein identification. Methods in Molecular Biology, 367. pp. 195-207. ISSN 1064-3745

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Official URL: http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=...

Abstract/Summary

Proteins are commonly identified through enzymatic digestion and generation of short sequence tags or fingerprints of peptide masses by mass spectrometry. Separation methods, such as liquid chromatography and electrophoresis, are often used to fractionate complex protein or peptide mixtures and these separations also provide information on the different species, such as molecular weight and isoelectric point from electrophoresis and hydrophobicity in reversed-phase chromatography. These are also properties that can be predicted from amino acid sequences derived from genomic sequences and used in protein identification. This chapter reviews recently introduced methods based on retention time prediction to extract information from chromatographic separations and the applications to protein identification in organisms with small and large genomes. Novel data on retention time prediction of posttranslationally modified peptides is also presented.

Item Type:Article
Refereed:Yes
Divisions:Faculty of Life Sciences > School of Biological Sciences
ID Code:10063
Uncontrolled Keywords:Amino Acid Sequence, Amniotic Fluid/chemistry, Chromatography, Liquid, Fungal Proteins/analysis/chemistry, Linear Models, Mass Spectrometry, Molecular Sequence Data, Pattern Recognition, Automated, Proteins/*analysis/chemistry, Reproducibility of Results, Software, Time Factors

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