Fluorine NMR study of proline-rich sequences using fluoroprolines

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

doi:https://doi.org/10.5194/mr-2-795-2021

Articles | Volume 2, issue 2

https://doi.org/10.5194/mr-2-795-2021

© Author(s) 2021. This work is distributed under
the Creative Commons Attribution 4.0 License.

Special issue:

Geoffrey Bodenhausen Festschrift

https://doi.org/10.5194/mr-2-795-2021

© Author(s) 2021. This work is distributed under
the Creative Commons Attribution 4.0 License.

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

Supplement

https://doi.org/10.5194/mr-2-795-2021-supplement

Data sets

Fluorine NMR study of proline-rich sequences using fluoroprolines Bruno Kieffer, Abir Ben Bouzayene, and Davy Sinnaeve https://doi.org/10.5281/zenodo.5548094

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.