Molecular dynamics for computational proteomics of methylated histone H3

• Published in: Biochimica et biophysica acta Vol. 1850; no. 5; pp. 1026 - 1040
• Main Authors: Grauffel, Cédric, Stote, Roland H., Dejaegere, Annick
• Format: Journal Article
• Language: English
• Published: Netherlands Elsevier B.V 01.05.2015; Elsevier
• Subjects: Animals; Binding Sites; Biochemistry; Biochemistry, Molecular Biology; Energy Transfer; Epigenetics; Histone; histones; Histones - chemistry; Histones - metabolism; Humans; Life Sciences; Lysine; Methylation; Molecular dynamics; Molecular Dynamics Simulation; post-translational modification; prediction; Protein Binding; Protein interaction; Protein Interaction Mapping - methods; Protein Processing, Post-Translational; Protein Structure, Tertiary; Proteomics; Proteomics - methods; Reproducibility of Results; sequence analysis; Transcription Factors - chemistry; Transcription Factors - metabolism; Molecular dynamics; Epigenetics; Protein interaction; Histone; Proteomics

Post-translational modifications of histones, and in particular of their disordered N-terminal tails, play a major role in epigenetic regulation. The identification of proteins and proteic domains that specifically bind modified histones is therefore of paramount importance to understand the molecul...