Role of Fine Structural Dynamics in Recognition of Histone H3 by HP1γ(CSD) Dimer and Ability of Force Fields to Describe Their Interaction Network
Author:
Affiliation:
1. Institute of Biophysics of the Czech Academy of Sciences, Královopolská 135, 612 65 Brno, Czech Republic
2. National Centre for Biomolecular Research, Faculty of Science, Masaryk University, Kamenice 5, 625 00 Brno, Czech Republic
Funder
Grantov? Agentura Cesk? Republiky
Publisher
American Chemical Society (ACS)
Subject
Physical and Theoretical Chemistry,Computer Science Applications
Link
https://pubs.acs.org/doi/pdf/10.1021/acs.jctc.9b00434
Reference93 articles.
1. The HP1 protein family: getting a grip on chromatin
2. HP1a: a structural chromosomal protein regulating transcription
3. Does heterochromatin protein 1 always follow code?
4. Coordinated methyl and RNA binding is required for heterochromatin localization of mammalian HP1α
5. HP1 binding to native chromatin in vitro is determined by the hinge region and not by the chromodomain
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2. Residues flanking the ARKme3T/S motif allow binding of diverse targets to the HP1 chromodomain: Insights from molecular dynamics simulations;Biochimica et Biophysica Acta (BBA) - General Subjects;2021-01
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