Effect of n-alcohols on the structure and stability of the Drosophila odorant binding protein LUSH.

@article{Bucci2006EffectON,
  title={Effect of n-alcohols on the structure and stability of the Drosophila odorant binding protein LUSH.},
  author={Brigid K Bucci and Schoen W Kruse and Anna B Thode and Sylvia M Alvarado and David N. M. Jones},
  journal={Biochemistry},
  year={2006},
  volume={45 6},
  pages={1693-701}
}
LUSH is an odorant binding protein expressed in the olfactory organs of Drosophila melanogaster that is required for the detection of alcohol in adult flies. Here we demonstrate that, in the absence of ligand, in vitro LUSH exists in a partial molten globule state. The presence of short-chain n-alcohols at pharmacologically relevant concentrations less than 50 mM shifts the conformational equilibrium to a more compact state that exhibits reduced binding of the fluorescent dye 1-anilino-8… CONTINUE READING

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