It may also be useful to look at homologues of the protein of interest, as sometimes Alphafold shows very different domain arrangements despite close sequence similarity.
John On Mon, Apr 4, 2022 at 3:17 PM Andrew Lovering <a.lover...@bham.ac.uk> wrote: > Hi Scott > We have obtained a structure of a flexible clamshell like fold only after > using a disulphide mutant to lock the domains based on a Rosetta Fold model. > Interestingly, Alphafold put the very same residues further apart > (probably a relevant "open" pose) > > Andy > > ------------------------------ > > 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/
