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PreprintAll rights reservedbioRxiv

NMR-measured Per-residue Electrostatic Potentials Reveal the Importance of Arginine-Lysine Balance on the Conformational Ensemble of Disordered Histone H3 Tails in Nucleosome Core Particles

  • A. Estelle
  • V. Schnapka
  • N. Bolik-Coulon
  • M. Bonomi
  • L. Kay1
  1. 1University of Toronto
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Cite

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BibTeX
@misc{estelle2026nmrmeasured,
  title = {{NMR-measured Per-residue Electrostatic Potentials Reveal the Importance of Arginine-Lysine Balance on the Conformational Ensemble of Disordered Histone H3 Tails in Nucleosome Core Particles}},
  author = {A. Estelle and V. Schnapka and N. Bolik-Coulon and M. Bonomi and L. Kay},
  howpublished = {bioRxiv},
  year = {2026},
  month = oct,
  doi = {10.64898/2026.10.25.761679},
  url = {https://www.biorxiv.org/content/10.64898/2026.10.25.761679v1},
}
RIS
TY  - UNPB
TI  - NMR-measured Per-residue Electrostatic Potentials Reveal the Importance of Arginine-Lysine Balance on the Conformational Ensemble of Disordered Histone H3 Tails in Nucleosome Core Particles
AU  - A. Estelle
AU  - V. Schnapka
AU  - N. Bolik-Coulon
AU  - M. Bonomi
AU  - L. Kay
PY  - 2026
DA  - 2026/10/25
PB  - bioRxiv
DO  - 10.64898/2026.10.25.761679
UR  - https://www.biorxiv.org/content/10.64898/2026.10.25.761679v1
ER  -