The Recognition Specificity of the CHD1 Chromodomain with Modified Histone H3 Peptides

Histone tail peptides comprise the flexible portion of chromatin, the substance which serves as the packaging for the eukaryotic genome. According to the histone code hypothesis, reader protein domains (chromodomains) can recognize modifications of amino acid residues within these peptides, regulati...

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Veröffentlicht in:	Journal of molecular biology 2011-02, Vol.406 (3), p.527-541
Hauptverfasser:	Stein, Richard S.L., Wang, Wei
Format:	Artikel
Sprache:	eng
Schlagworte:	amino acids Animals binding capacity chromatin Computer Simulation DNA Helicases - chemistry DNA Helicases - metabolism DNA-binding proteins DNA-Binding Proteins - chemistry DNA-Binding Proteins - metabolism free-energy calculation genes histone code histones Histones - chemistry Histones - metabolism Humans Methylation Mice MM–GBSA Models, Molecular molecular dynamics peptides Protein Binding Protein Conformation protein recognition Protein Structure, Tertiary surface area
Online-Zugang:	Volltext
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