Based on this paper
Article The P1 ' specificity of tobacco etch virus protease
,TEV protease can cleave between the Gln and several amino-acids (besides Gly/Ser) with acceptable efficiency in its recognition site.
Therefore, it's practically possible to purify many proteins (without an extra residue at the N-terminal end), by using affinity chromatography.
I was wondering if anyone could share their experience/knowledge using TEV protease to cleave between Gln and Met?
Sorry, I have no experience with the specific case of Q/M cleavage, but remember that most proteins whose second residue is a small sidechain aminoacid actually have their N-terminal methionine removed by MAP while still being elongated in the ribosome.
Alejandro Martin Thanks for your comment. I edited my question.
I'm actually interested in finding a convenient/low-cost procedure for preparing a specific polypeptide with a methionine residue at its N-terminal end, using ni-nta affinity chromatography.
Paul Weber in my opinion a SUMO fusion would be a better alternative.
Alejandro Martin It's an amyloid protein, and I'm worried that using sumo protease would affect the aggregation process.
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