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[ahitron]

Hi all, I'm using a dimedone-based probe to tag proteins with specific cysteine modifications.  An article I recently came across that looked at the binding efficiency of this tag under different pH, and they found that the probe was much more efficient at binding to sulfenic acid-cysteines at low pH (~5.5).  Since the cysteine sulfenic acid is already very labile, I want to make sure that I have the most efficient binding conditions I can, but I'm a little concerned about using a mildly acidic lysis buffer.  So, I was wondering if anyone had any advice on the use of low-pH cell lysis conditions.  Would the low pH hurt my lysis, or alter the composition of the lysate (aside from possible denaturation)?