Magnetic Resonance Center and Department of Chemistry
University of Florence

Via L. Sacconi 6
50019 Sesto Fiorentino, (FI) -Italy

Tel: +39 055 4574243
e-mail: felli[at]cerm.unifi.it ; isabellacaterina.felli[at]unifi.it

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Neglected for a long time, highly flexible, intrinsically disordered proteins (IDPs), as well as flexible regions of complex protein machineries (IDRs), recently attracted the attention of the scientific community. Research in this field is blooming. Novel functional modules that are not yet described in the protein data bank (PDB) are beginning to be discovered. This is likely to be just a glimpse on the versatility through which function is encoded in the primary sequence of proteins not only through structure but also through disorder and flexibility. Many of the currently incurable diseases, such as cancer and neurodegenerative diseases, originate by misfuction of complex proteins lacking a stable three dimensional structure. The potential impact of shifting the focus to IDPs/IDRs as targets for drug discovery is extraordinary. To fully realize this objective a thorough understanding of their structural and dynamic properties is required.

Fascinated by this emerging field of research I like to contribute to it by development of improved NMR methods to exploit at best this highly powerful, sophisticated spectroscopic technique to look at intimate details of IDPs/IDRs.

A recent talk within the "Emerging Topics in Biomolecular Magnetic Resonance" is available at:

Full CV






Taking Simultaneous Snapshots of Intrinsically Disordered Proteins in Action.
Schiavina M, Murrali MG, Pontoriero L, Sainati V, Kümmerle R, Bermel W, Pierattelli R, Felli IC. Biophys J. 2019, 117:46-55. doi: 10.1016/j.bpj.2019.05.017.

NMR Characterization of Long-Range Contacts in Intrinsically Disordered Proteins from Paramagnetic Relaxation Enhancement in 13 C Direct-Detection Experiments.
Mateos B, Konrat R, Pierattelli R, Felli IC. Chembiochem. 2019, 20:335-339. doi: 10.1002/cbic.201800539.

The Ambivalent Role of Proline Residues in an Intrinsically Disordered Protein: From Disorder Promoters to Compaction Facilitators.
Mateos B, Conrad-Billroth C, Schiavina M, Beier A, Kontaxis G, Konrat R, Felli IC, Pierattelli R. J Mol Biol. 2020, 432:3093-3111. doi: 10.1016/j.jmb.2019.11.015.

Sequence Context Influences the Structure and Aggregation Behavior of a PolyQ Tract.
Eftekharzadeh B, Piai A, Chiesa G, Mungianu D, García J, Pierattelli R, Felli IC, Salvatella X. Biophys J. 2016, 110:2361-2366. doi: 10.1016/j.bpj.2016.04.022.

Just a Flexible Linker? The Structural and Dynamic Properties of CBP-ID4 Revealed by NMR Spectroscopy.
Piai A, Calçada EO, Tarenzi T, Grande AD, Varadi M, Tompa P, Felli IC, Pierattelli R. Biophys J. 2016, 110:372-381. doi: 10.1016/j.bpj.2015.11.3516.

Novel methods based on (13)C detection to study intrinsically disordered proteins.
Felli IC, Pierattelli R. J Magn Reson. 2014, 241,115-25. doi: 10.1016/j.jmr.2013.10.020.

In-cell ¹³C NMR spectroscopy for the study of intrinsically disordered proteins.
Felli IC, Gonnelli L, Pierattelli R. Nat Protoc. 2014, 9:2005-16. doi: 10.1038/nprot.2014.124.

"CON-CON" assignment strategy for highly flexible intrinsically disordered proteins.
Piai A, Hošek T, Gonnelli L, Zawadzka-Kazimierczuk A, Koźmiński W, Brutscher B, Bermel W, Pierattelli R, Felli IC. J Biomol NMR. 2014, 60:209-18. doi: 10.1007/s10858-014-9867-6.

NMR spectroscopic studies of intrinsically disordered proteins at near-physiological conditions.
Gil S, Hošek T, Solyom Z, Kümmerle R, Brutscher B, Pierattelli R, Felli IC. Angew Chem Int Ed Engl. 2013, 52:11808-12. doi: 10.1002/anie.201304272.

Intrinsically Disordered Proteins Studied by NMR Spectroscopy.
Felli, I. C.; Pierattelli, R. Eds., Springer, 2015. https://doi.org/10.1007/978-3-319-20164-1.