Macromolecular crowding induces a molten globule state in the C-terminal domain of histone H1.

@article{Roque2007MacromolecularCI,
  title={Macromolecular crowding induces a molten globule state in the C-terminal domain of histone H1.},
  author={Alicia Roque and Inma Ponte and Pedro Suau},
  journal={Biophysical journal},
  year={2007},
  volume={93 6},
  pages={2170-7}
}
We studied the secondary structure of the C-terminal domains of the histone H1 subtypes H1 degrees (C-H1 degrees ) and H1t (C-H1t) in the presence of macromolecular crowding agents (Ficoll 70 and PEG 6000) by IR spectroscopy. The carboxyl-terminal domain has little structure in aqueous solution but became extensively folded in the presence of crowding agents. In 30% PEG, C-H1 degrees contained 19% alpha-helix, 28% beta-sheet, 16% turns, and 31% open loops. Similar proportions were observed in… CONTINUE READING