Disulphide bridges which are formed between sulphur atoms of two cysteine residues play crucial role in creating and stabilizing the tertiary structure of proteins (intrachain bridges). Additionally by having an impact on the covalent bond of the protein subunits (interchain bridges) they ensure the correct protein folding and thus their proper function.

By applying the methods of mass spectrometry and liquid chromatography we offer the possibility to identify the number and location of disulphide bridges as well as free sulphydryl groups in proteins and peptides.

Analiza mostków dwusiarczkowych

Contact

Dorota Stadnik, Ph.D.
phone:  +48 22 37 86 155
stadnikd@iba.waw.pl

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Anna Bierczyńska-Krzysik, Ph.D.
phone: +48 22 37 86 232
bierczynskaa@iba.waw.pl

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Piotr Baran, M.Sc.
phone: +48 22 37 86 232
baranp@iba.waw.pl