Sorry for a non-ccp4 question. We have determined a structure which is mainly a coiled coil motif. The two helices are from the same protein chain linked by a short turn.
However, the SAXS data indicates that "this protein is probably natively unfolded or may have very flexible domains and linkers" as commented by our collaborators who did the SAXS experiments. Could this be due to the "shifting" of the turn connecting the two helices? Has this kind of "flexibility" in the turn position in a coiled coil motif been observed in other coiled coil structures? Thank you Rongjin Guan
