Hill Coefficient Analysis of Transmembrane Helix Dimerization

@article{Soong2009HillCA,
  title={Hill Coefficient Analysis of Transmembrane Helix Dimerization},
  author={Ricky Kai Soong and Mikhail Merzlyakov and Kalina Hristova},
  journal={Journal of Membrane Biology},
  year={2009},
  volume={230},
  pages={49-55}
}
  • Ricky Kai Soong, Mikhail Merzlyakov, Kalina Hristova
  • Published 2009
  • Medicine, Chemistry
  • Journal of Membrane Biology
  • Here, we employed the Hill equation, used broadly to characterize cooperativity in protein–ligand binding, to describe the dimerization of transmembrane (TM) helices in hydrophobic environments. The Hill analysis of wild-type fibroblast growth factor receptor 3 (FGFR3) TM domain dimerization gives a Hill coefficient of ~1 for lipid bilayers but only ~0.2 for sodium dodecyl sulfate (SDS) micelles. We propose that this finding is indicative of heterogeneity in FGFR3 TM dimer structure and… CONTINUE READING

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