Automated Calculation of Unique Peptide Sequences for Unambiguous
Identification of Highly Homologous Proteins by Mass Spectrometry |
Michael Kohl*, Gorden Redlich*, Martin Eisenacher, Anke Schnabel, Helmut E. Meyer, Katrin Marcus and Christian Stephan |
| Medizinisches Proteom-Center, Ruhr-Universität Bochum, Bochum, Germany |
| Corresponding author: |
Michael Kohl, Medizinisches Proteom-Center, ZKF E.2.051, Ruhr-Universitaet Bochum, Bochum, Universitaetsstr. 150, D-44801 Bochum, Germany
Phone: +49-234-32-29275;
Fax: +49-234-32-14554
E-mail: Michael.Kohl@rub.de |
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| *Both authors contributed equally to this work. |
| Received April 03, 2008; Accepted April 09, 2008; Published April 20, 2008 |
| Citation: Michael K, Gorden R, Martin E, Anke S, Helmut EM, etal. (2008) Automated Calculation of Unique Peptide
Sequences for Unambiguous Identification of Highly Homologous Proteins by Mass Spectrometry. J Proteomics Bioinform 1:
006-010. doi:10.4172/jpb.1000003 |
| Copyright: © 2008 Michael K, etal. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. |
| Abstract |
In regular proteomics approaches proteases are used to digest the proteome into a set of peptides. Unfortunately, determining proteins
on the basis of peptides implies some uncertainty since a peptide may be part of different proteins. Therefore, a targeted detection of
unique peptides of particular proteins is a promising task for an unambiguous identification of a specific protein. Here we present a
software solution that offers the possibility for a highly efficient and simple detection of such unique peptides. In a first step a SQL-based
database of theoretically digested peptides from a given FASTA file formatted protein database is generated by choosing a protease. In a
second step, in silico generated peptides from a pre-defined protein sequence are compared to this peptide database in order to identify
unique peptides. Amongst others, possible applications are identification of proteins when only sparse peptide information is available
or advanced proteomics techniques that require information about the uniqueness of peptides such as Multiple Reaction Monitoring
(MRM). |
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