Conformational changes in actin induced by its interaction with gelsolin.

  title={Conformational changes in actin induced by its interaction with gelsolin.},
  author={Sofia Yu Khaitlina and Horst Hinssen},
  journal={Biophysical journal},
  volume={73 2},
Actin cleaved by the protease from Escherichia coli A2 strain between Gly42 and Val43 (ECP-actin) is no longer polymerizable when it contains Ca2+ as a tightly bound cation, but polymerizes when Mg2+ is bound. We have investigated the interactions of gelsolin with this actin with regard to conformational changes in the actin molecule induced by the binding of gelsolin. ECP-(Ca)actin interacts with gelsolin in a manner similar to that in which it reacts with intact actin, and forms a… CONTINUE READING
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