An amphipathic alpha-helix at a membrane interface: a structural study using a novel X-ray diffraction method.

@article{Hristova1999AnAA,
  title={An amphipathic alpha-helix at a membrane interface: a structural study using a novel X-ray diffraction method.},
  author={Kalina Hristova and William C. Wimley and Vinod K. Mishra and G M Anantharamiah and Jere P. Segrest and Stephen H White},
  journal={Journal of molecular biology},
  year={1999},
  volume={290 1},
  pages={
          99-117
        }
}
The amphipathic alpha-helix is a recurrent feature of membrane-active proteins, peptides, and toxins. Despite extensive biophysical studies, the structural details of its affinity for membrane interfaces remain rather vague. We report here the first results of an effort to obtain detailed structural information about alpha-helices in membranes by means of a novel X-ray diffraction method. Specifically, we determined the transbilayer position and orientation of an archetypal class A amphipathic… 
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