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
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