de Novo Sequence Analysis of N-Terminal Sulfonated Peptides After in-Gel Guanidination

In this protocol, we describe an approach in which two-dimensional electrophoresis (2DE)-separated proteins are guanidinated in-gel prior to enzymatic cleavage. In contrast to previously described techniques, this procedure allows the extracted tryptic peptides to be N-terminally sulfonated without any further sample purification. The protocol was applied on a proteomic study of 2DE-separated proteins fromHalorhodospira halophila, an extremophilic eubacterium with an unsequenced genome at the moment of analysis.

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