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Hi, dear colleagues! Looking for your opinion! During perform 2D we suspest acrylamide and cystein group interactions leading to artefact results. When we perform 1D the same sample we got a lot of strips, but in 2D we have just a lot of spots and spindles on one level... Could you propose something? How can we prove or disprove that? And what do you think, how we can improve quality of ...

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... site. Here, we investigate the effect on recognition of protein targets of placing an unnatural electrophile adjacent to the target binding site. We positioned a weak electrophile, acrylamide, near the binding site between an affibody, a non-immunoglobulin binding scaffold, and its protein target. The proximity between cysteine, lysine, or histidine on the target protein drove covalent bond ...

... without tryptophan and then grown in YPD medium to mid-exponential phase. Whole cell lysates were cleared by centrifugation at 14 000 g. Resulting supernatants were separated on NuPAGE acrylamide gels (Invitrogen) and electrophoretically transferred onto a PVDF membrane (Invitrogen). Removal of redundant structures was achieved using the PISCES server (Wang and Dunbrack, 2005) with the following ...