Contribution of hydrophobic interactions to the folding and fibrillation of histone H1 and its carboxy-terminal domain.

@article{Roque2012ContributionOH,
  title={Contribution of hydrophobic interactions to the folding and fibrillation of histone H1 and its carboxy-terminal domain.},
  author={Alicia Roque and Nuria Teruel and Rita L{\'o}pez and Inma Ponte and Pedro Suau},
  journal={Journal of structural biology},
  year={2012},
  volume={180 1},
  pages={101-9}
}
Histone H1 is involved in chromatin structure and gene regulation. H1 also performs functions outside cell nuclei, which may depend on its properties as a lipid-binding protein. The H1 CTD behaves as an intrinsically disordered protein (IDP) with coupled binding and folding. Here, we used neutral detergents and anionic SDS to study the contribution of hydrophobic interactions to the folding of the CTD. In the presence of neutral detergents, the CTD folded with proportions of secondary structure… CONTINUE READING