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          Institute: MPI für Infektionsbiologie     Collection: Core Facilites     Display Documents

ID: 399860.0, MPI für Infektionsbiologie / Core Facilites
The speciation of the proteome
Authors:Jungblut, Peter R.; Holzhütter, Hermann-Georg; Apweiler, Rolf; Schlüter, Hartmut
Date of Publication (YYYY-MM-DD):2008-07-18
Title of Journal:Chemistry Central Journal
Journal Abbrev.:Chem. Cent. J.
Sequence Number of Article:16
Copyright:© 2008 Jungblut et al
This is an open access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
Review Status:Peer-review
Audience:Experts Only
Abstract / Description:Abstract

In proteomics a paradox situation developed in the last years. At one side it is basic knowledge that proteins are post-translationally modified and occur in different isoforms. At the other side the protein expression concept disclaims post-translational modifications by connecting protein names directly with function.

Optimal proteome coverage is today reached by bottom-up liquid chromatography/mass spectrometry. But quantification at the peptide level in shotgun or bottom-up approaches by liquid chromatography and mass spectrometry is completely ignoring that a special peptide may exist in an unmodified form and in several-fold modified forms. The acceptance of the protein species concept is a basic prerequisite for meaningful quantitative analyses in functional proteomics. In discovery approaches only top-down analyses, separating the protein species before digestion, identification and quantification by two-dimensional gel electrophoresis or protein liquid chromatography, allow the correlation between changes of a biological situation and function.

To obtain biological relevant information kinetics and systems biology have to be performed at the protein species level, which is the major challenge in proteomics today.
External Publication Status:published
Document Type:Article
Communicated by:Hilmar Fünning
Affiliations:MPI für Infektionsbiologie/Core Facilities
External Affiliations:European Bioinformat Inst, Cambridge CB10 1SD, England.; Inst Biochem, Charite Berlin, Berlin, Germany.
Identifiers:ISI:000259067800001 [ID No:1]
ISSN:1752-153X [ID No:2]
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