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Proteomics


The dream of having the human genome completely sequenced is now a reality. However, the proteins generated from a given genome are much more complex than the corresponding genome itself. In humans, for example, about half a million proteins are generated from some 30 000 genes. Moreover, the proteome is, is unlike the genome, changing with environment, age, disease and many other known and unknown factors and is therefore a function of the specific conditions the cell; tissue or organism is and has been subjected to. Many proteins are also modified after their synthesis, leading to molecules with different biological activity. The expression levels of these protein ”isoforms” are often differentially regulated in space and time or in healthy and diseased states. Thus, the proteome is a highly complex and dynamic protein network generated from an essentially static genomic blueprint.
Proteomics is a new scientific discipline that focuses on the global study of proteins: their roles, structures, localisation, interactions, and other factors. Proteomics can be defined as the qualitative and quantitative comparison of proteomes under different conditions. Our goal is to identify potential proteins linked to neurodegenerative diseases. The main strategy is comparative proteomics studies, where two proteomes are compared and differences due to genetic variations, culture conditions, diseases or drug treatment, are detected. This strategy yields a limited number of biomarker candidates, which can be identified, characterised and quantitated.

Our aim is to


• define protein expression patterns that can serve as diagnostic and prognostic markers for neurodegenerative diseases
• identify, characterise and quantitate differently expressed proteins/protein isoforms

Our tools are


preparative/analytical gel electrophoresis, and liquid chromatography for protein separation and sample pre-fractionation
MALDI-TOFMS/MS, and ESI-IT/FTICRMS/MS for identification and characterisation of post-translational modifications
ESI-QqQMS, MALDI-TOFMS, and ESI-IT/FTICRMS for quantitation

 

 

 

Page Manager: Staffan Persson|Last update: 8/2/2010
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