Conformational dimorphism and transmembrane orientation of prion protein residues 110-136 in bicelles.

@article{Glover2001ConformationalDA,
  title={Conformational dimorphism and transmembrane orientation of prion protein residues 110-136 in bicelles.},
  author={Kerney Jebrell Glover and Jennifer A Whiles and Matthew J. Wood and Giuseppe Melacini and Elizabeth A. Komives and Regitze R. Vold},
  journal={Biochemistry},
  year={2001},
  volume={40 44},
  pages={13137-42}
}
A fragment corresponding to the putative membrane-associating domain of the prion protein (residues 110-136) was analyzed in phospholipid bicelles. Prion(110-136) associated with bicelles and exhibited a lipid- and pH-dependent conformational dimorphism between unstructured (pH 4.5) and alpha-helical (pH 7.5). Mutational analysis indicated that the charge state of a single histidine residue was largely responsible for the dimorphism. Amide-lipid NOEs and amide-water chemical exchange… CONTINUE READING

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