Hi Erik, A couple of things to consider: 1. Begin the N-terminus from helix "initiating" residues (i.e. one residue overhang might not be sufficient) 2. If not done already, add the 6-carboxy-fluorescein moiety at C-terminus of the peptide Good Luck, Partha
On Wed, Mar 20, 2024 at 6:03 AM Erik Debler <[email protected]> wrote: > Hi everyone, > > Sorry for the off-topic question, but I thought I may get some > advice/pointers about the design of a stable alpha-helical peptide. I would > like to obtain a peptide mimicking a 13-residue alpha-helix that was > identified in a protein to mediate a protein-protein interaction, which is > completely abolished by three spatially adjacent point mutations in the > helix of the protein. I designed a peptide with a 1-residue overhang on > each side and a 6-carboxy-fluorescein moiety on one end, but the peptide > did not bind to the interaction partner probed by fluorescence > polarization. The peptide easily dissolves in water, so solubility does not > seem to be an issue. Any suggestions or pointers to relevant literature > would be greatly appreciated. > > Cheers! > Erik > > ------------------------------ > > To unsubscribe from the CCP4BB list, click the following link: > https://www.jiscmail.ac.uk/cgi-bin/WA-JISC.exe?SUBED1=CCP4BB&A=1 > ######################################################################## To unsubscribe from the CCP4BB list, click the following link: https://www.jiscmail.ac.uk/cgi-bin/WA-JISC.exe?SUBED1=CCP4BB&A=1 This message was issued to members of www.jiscmail.ac.uk/CCP4BB, a mailing list hosted by www.jiscmail.ac.uk, terms & conditions are available at https://www.jiscmail.ac.uk/policyandsecurity/
