Preprints
https://doi.org/10.5194/mr-2021-37
https://doi.org/10.5194/mr-2021-37

  12 Apr 2021

12 Apr 2021

Review status: this preprint is currently under review for the journal MR.

Exclusively heteronuclear NMR experiments for the investigation of intrinsically disordered proteins: focusing on proline residues

Isabella C. Felli1, Wolfgang Bermel2, and Roberta Pierattelli1 Isabella C. Felli et al.
  • 1CERM Department of Chemistry ‘‘Ugo Schiff’’, University of Florence, Via Luigi Sacconi 6, 50019 Sesto Fiorentino, Florence, Italy
  • 2Bruker BioSpin GmbH, Silberstreifen, 76287 Rheinstetten, Germany

Abstract. NMR represents a key spectroscopic technique to contribute to the emerging field of highly flexible, intrinsically disordered proteins (IDPs) or protein regions (IDRs) that lack a stable three-dimensional structure. A set of exclusively heteronuclear NMR experiments tailored for proline residues, highly abundant in IDPs/IDRs, are presented here. They provide a valuable complement to the widely used approach based on amide proton detection, filling the gap introduced by the lack of amide protons in prolines within polypeptide chains. The novel experiments have very interesting properties for the investigations of IDPs/IDRs of increasing complexity.

Isabella C. Felli et al.

Status: open (until 10 May 2021)

Comment types: AC – author | RC – referee | CC – community | EC – editor | CEC – chief editor | : Report abuse
  • RC1: 'Comment on mr-2021-37', Anonymous Referee #1, 26 Apr 2021 reply
  • RC2: 'Comment on mr-2021-37', Anonymous Referee #2, 30 Apr 2021 reply

Isabella C. Felli et al.

Isabella C. Felli et al.

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Short summary
NMR represents a key spectroscopic technique to study intrinsically disordered proteins (IDPs) that lack a stable three-dimensional structure. We present a set of NMR experiments tailored for proline residues, highly abundant in IDPs. The novel experiments have very interesting properties for the investigation of IDPs of increasing complexity.