Scientists develop new method to identify glycosylated proteins
14 June 2010
Various processes in our body are controlled by subsequent changes of proteins.
Therefore, the identification of such modifications is essential for the further exploration of our organism. Now, scientists of the Max Planck Institute of Biochemistry in Martinsried, Germany, have made a crucial contribution to this:
Using a new method, they have been able to identify more than 6,000 glycosylated protein sites in different tissues and have thus established an important basis for the better understanding of all life processes (Cell, May 28, 2010).
Many biological mechanisms like immune response, apoptosis or pathogenesis of diseases are based on the subsequent transformation of single components of proteins, the amino acids.
Scientists call this process ''posttranslational protein modification''. Although the technologies in proteomics have developed rapidly in the last years, until now the identification of such modified proteins was only possible with limitations.
Particularly, the transformation of proteins by glycosylation – carbohydrates binding to single amino acids – has been widely unexplored.