alpha-Bungarotoxin binding to two acetylcholine receptor alpha-peptides and their methylmercury-modified analogs: intrinsic phosphorescence and optically detected magnetic resonance studies.

@article{Schlyer1992alphaBungarotoxinBT,
  title={alpha-Bungarotoxin binding to two acetylcholine receptor alpha-peptides and their methylmercury-modified analogs: intrinsic phosphorescence and optically detected magnetic resonance studies.},
  author={B D Schlyer and August H. Maki and Edward Hawrot},
  journal={FEBS letters},
  year={1992},
  volume={297 1-2},
  pages={87-90}
}
Phosphorescence and optically detected magnetic resonance (ODMR) have been used to characterize two synthetic peptides, alpha 181-198 and alpha 185-196, of the major binding determinant of the alpha-acetylcholine receptor (AChR) of Torpedo californica and its interaction with alpha-bungarotoxin (BgTX) using Trp as an intrinsic probe. BgTX conformational… CONTINUE READING