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

Pub. Date : 2012 Oct

PMID : 22813934






4 Functional Relationships(s)
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1 Here, we used neutral detergents and anionic SDS to study the contribution of hydrophobic interactions to the folding of the CTD. Sodium Dodecyl Sulfate CTD Homo sapiens
2 The greatest effect was observed in the fully phosphorylated CTD (three phosphate groups) in the presence of anionic SDS (7:1, detergent/CTD molar ratio); in these conditions, the CTD became an all-beta protein, with 83% beta-structure and no alpha-helix. Sodium Dodecyl Sulfate CTD Homo sapiens
3 The greatest effect was observed in the fully phosphorylated CTD (three phosphate groups) in the presence of anionic SDS (7:1, detergent/CTD molar ratio); in these conditions, the CTD became an all-beta protein, with 83% beta-structure and no alpha-helix. Sodium Dodecyl Sulfate CTD Homo sapiens
4 The greatest effect was observed in the fully phosphorylated CTD (three phosphate groups) in the presence of anionic SDS (7:1, detergent/CTD molar ratio); in these conditions, the CTD became an all-beta protein, with 83% beta-structure and no alpha-helix. Sodium Dodecyl Sulfate CTD Homo sapiens