Effects of charge-modifying mutations in histone H2A α3-domain on nucleosome stability assessed by single-pair FRET and MD simulations
Author:
Publisher
Springer Science and Business Media LLC
Subject
Multidisciplinary
Link
http://www.nature.com/articles/s41598-017-13416-x.pdf
Reference44 articles.
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3. Davey, C. A., Sargent, D. F., Luger, K., Maeder, A. W. & Richmond, T. J. Solvent mediated interactions in the structure of the nucleosome core particle at 1.9 a resolution. J Mol Biol 319, 1097–1113 (2002).
4. Luger, K., Mäder, A. W., Richmond, R. K., Sargent, D. F. & Richmond, T. J. Crystal structure of the nucleosome core particle at 2.8 Å resolution. Nature 389, 251–260 (1997).
5. Nurse, N. P., Jimenez-Useche, I., Smith, I. T. & Yuan, C. Clipping of flexible tails of histones H3 and H4 affects the structure and dynamics of the nucleosome. Biophysical journal 104, 1081–1088, https://doi.org/10.1016/j.bpj.2013.01.019 (2013).
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