Articles | Volume 2, issue 2
Research article
09 Nov 2021
Research article |  | 09 Nov 2021

Fluorine NMR study of proline-rich sequences using fluoroprolines

Davy Sinnaeve, Abir Ben Bouzayene, Emile Ottoy, Gert-Jan Hofman, Eva Erdmann, Bruno Linclau, Ilya Kuprov, José C. Martins, Vladimir Torbeev, and Bruno Kieffer


Interactive discussion

Status: closed

Comment types: AC – author | RC – referee | CC – community | EC – editor | CEC – chief editor | : Report abuse
  • RC1: 'Comment on mr-2021-54', Ranajeet Ghose, 19 Jul 2021
    • AC1: 'Reply on RC1', Bruno Kieffer, 09 Sep 2021
  • RC2: 'Comment on mr-2021-54', Guy Lippens, 30 Jul 2021
    • AC2: 'Reply on RC2', Bruno Kieffer, 09 Sep 2021
  • RC3: 'Comment on mr-2021-54', Anonymous Referee #3, 10 Aug 2021
    • AC3: 'Reply on RC3', Bruno Kieffer, 09 Sep 2021

Peer review completion

AR: Author's response | RR: Referee report | ED: Editor decision
AR by Bruno Kieffer on behalf of the Authors (09 Sep 2021)  Author's response    Manuscript
ED: Publish subject to corrections (28 Sep 2021) by Fabien Ferrage
AR by Bruno Kieffer on behalf of the Authors (05 Oct 2021)  Author's response    Manuscript
Short summary
Fluorine NMR was used to study the interaction between a proline-rich peptide and a SH3 domain using 4S- and 4R-fluorinated prolines whose potential as NMR probes has not been exploited yet. We present a comprehensive study addressing several aspects to be considered when using these residues as NMR probes, including relaxation and dynamics. We show that their conformational bias may be used to modulate the kinetics of protein binding to proline-rich motifs.