Articles | Volume 2, issue 1
Research article
21 Apr 2021
Research article |  | 21 Apr 2021

Characterization of nucleosome sediments for protein interaction studies by solid-state NMR spectroscopy

Ulric B. le Paige, ShengQi Xiang, Marco M. R. M. Hendrix, Yi Zhang, Gert E. Folkers, Markus Weingarth, Alexandre M. J. J. Bonvin, Tatiana G. Kutateladze, Ilja K. Voets, Marc Baldus, and Hugo van Ingen


Interactive discussion

Status: closed

Comment types: AC – author | RC – referee | CC – community | EC – editor | CEC – chief editor | : Report abuse
  • RC1: 'Comment on mr-2021-21', Claudio Luchinat, 08 Mar 2021
    • AC1: 'Reply on RC1', Hugo van Ingen, 09 Mar 2021
  • RC2: 'Comment on mr-2021-21', Paul Schanda, 13 Mar 2021
    • AC2: 'Reply on RC2', Hugo van Ingen, 16 Mar 2021
  • RC3: 'Comment on mr-2021-21', Lars Nordenskiöld, 18 Mar 2021
    • AC3: 'Reply on RC3', Hugo van Ingen, 04 Apr 2021

Peer review completion

AR: Author's response | RR: Referee report | ED: Editor decision
AR by Hugo van Ingen on behalf of the Authors (04 Apr 2021)  Author's response    Author's tracked changes    Manuscript
ED: Publish as is (07 Apr 2021) by Jörg Matysik

Post-review adjustments

AA: Author's adjustment | EA: Editor approval
AA by Hugo van Ingen on behalf of the Authors (21 Apr 2021)   Author's adjustment   Manuscript
EA: Adjustments approved (21 Apr 2021) by Jörg Matysik
Short summary
NMR studies can be of great help in understanding the molecular mechanisms of nucleosome functions. For solid-state NMR, nucleosomes need to be tightly packed together. We show that centrifugation of nucleosomes results in formation of gels with very high packing ratios yet without pronounced order in the packing and without formation of specific or stable inter-nucleosome contacts. This makes the approach suitable also for the study of proteins that bind weakly to the nucleosome.