rbateman at wave.st.usm.edu (Dr. Robert Bateman) wrote:
>I have a small (100 aa) protein with a single cysteine which is active
>as a protease inhibitor in the monomer form. I am wondering if it is
>inactive in the disulfide-bonded dimeric form. I would like some suggestions
>on how to get it to form intermolecular disulfide bonds so I can test this.
>Bob Bateman
>rbateman at wave.st.usm.edu
I used to cyclize synthetic peptides by disolving them in a buffered
solution above pH 7.5 and letting them stir for a day or so. The
disolved oxygen oxidized the Cys residues into disulfides.
