Hi All,

I'm trying to manually model a linker region using computational information (such as which residues are predicted to be in helical form, etc.). I have the sequence in PyMOL as an unmodeled linear chain (or whatever the program chose to do with bond angles when I manually generated the sequence). I'm now trying to force specific lengths of residues to take the alpha-helical form in that area. Is there any way to do so? And if I do, would PyMOL automatically manipulate the atoms in space to have sensical placements as to minimize clashes, or would it just forcibly twirl that section into a helix?

Thanks,

Alex