.

In cooperation with DECODON we give a webinar on Redox proteomics on May 07, 2013. The talk will be given by Jan Heise, PhD, in three sessions at

10 am CET (Berlin time) in German Registration

.

3 pm CET (Paris time) in English Registration

.

12 am EST (New York time) in English Registration

.

and will take about half an hour plus time for discussion.

.

.

Abstract

Redox-Proteomics: Stress Response and Cellular Signaling

In living cells biotic and abiotic stress is tightly related to production and scavenging of reactive oxygen and nitrogen species (ROS/NOS). Due to their high chemical reactivity oxygen and nitrogen species can oxidize various biological molecules such as unsaturated lipids, carbohydtrates, nucleic acids, but mostly, due to their high abundancy, proteins.

In proteins the thiol group of the amino acid cysteine is a primary target for oxidation events. The other sulfur-containg amino acid methionine and the aromatic amino acids tyrosine and tryptophane are targets for oxidation to a lesser extent (less reactive).

During the last decade it became clear that protein oxidaztion is not an irreversible process only. There is much evidence, that reversible oxidative and nitrosative modification of proteins play a central role in the complex protein network. Therefore, particulary thiol oxidation occurs not only due to stress conditions but plays an important part in the redox signaling pathway.

2D gel-based top-down proteomic approaches offer both, the careful separation of complex protein samples as well as the easy visualization of protein modifications. Saturn-2D™ REDOX is a novel technology for the visualization of thiol modifications of proteins in complex samples. Samples differing in their REDOX potential are specifically Cys-labeled and then compared. The existing problem of inconsistent spot matching – unequal binding of fluorescent dyes to proteins differing in their REDOX potential – is solved by a special Cys-interacting compound (CinC).