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.
|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|
|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]