Magnetic Resonance Center and Department of Chemistry

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

Tel: +39 055 4574239
e-mail: schiavina[at]

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Marco Schiavina was born in 1993. In 2015 he obtained his Bachelor’s degree in Chemistry at the University of Ferrara and in 2018 his Master's degree in Chemistry at the University of Florence. In the same year, he won a Ph.D. scholarship in the International Doctorate in Structural Biology at CERM at the University of Florence.
During his Ph.D. period, he started working on the development and application of 13C-direct detected experiments for the study of Intrinsically Disordered Proteins (IDPs).
To easily obtain the sequence-specific assignment of α-synuclein, a set of multidimensional experiments (3D, 4D and 5D) were implemented exploiting the Automated Projection SpectroscopY (APSY) strategy. The same strategy was then applied to investigate the N-terminal domain of the phosphoprotein from the Nipah virus (NiV-PNT), a 606 residue-long disordered protein.
With the same aim of developing new NMR techniques for the study of IDPs, a series of 13C-detected experiments exploiting the Multiple Receiver technology were first set-up and applied to investigate systems with different extents of complexity.
The identification of novel characteristic motifs, responsible for various properties of IDPs was also a matter of study in the investigation of the interaction of α-synuclein with metal ions as well as to identify the driving forces of the compact state characterizing the Osteopontin protein.
In 2021 Marco won a postdoctoral position at CERM with the aim of studying the interaction of multidomain proteins, macromolecules composed of the concomitant presence of globular and disordered domains, with various partners. In this context, the Multiple Receiver strategy was applied to investigate the interplay between the Nucleocapsid protein from the SARS-CoV 2 virus with RNA.
Since December 2022 Marco has been enrolled as a researcher at the University of Florence working at CERM in the framework of the ITACA.SB project in order to expand services for Nuclear Magnetic Resonance at CERM/CIRMMP.



NMR; Carbon detection; intrinsically disordered proteins; multidomain proteins



Studies of proline conformational dynamics in IDPs by 13C-detected cross-correlated NMR relaxation
M Schiavina, R Konrat, I Ceccolini, B Mateos, R Konrat, IC Felli, R Pierattelli
Journal of Magnetic Resonance, 107539, 2023

NMR reveals specific tracts within the intrinsically disordered regions of the SARS-CoV-2 nucleocapsid protein involved in RNA encountering
L Pontoriero, M Schiavina, SM Korn, A Schlundt, R Pierattelli, IC Felli
Biomolecules 12 (7), 929, 2022

Large-scale recombinant production of the SARS-CoV-2 proteome for high-throughput and structural biology applications
…, R Riek, CM Rienstra, A Robertson, AS Pinheiro, R Sabbatella, N Salvi, K Saxena, L Schulte, M Schiavina…
Frontiers in molecular biosciences 8, 89, 2021

The highly flexible disordered regions of the SARS-CoV-2 nucleocapsid N protein within the 1–248 residue construct: sequence-specific resonance assignments through NMR
M Schiavina, L Pontoriero, VN Uversky, IC Felli, R Pierattelli
Biomolecular NMR Assignments 15 (1), 219-227, 2021

Ensemble description of the intrinsically disordered N-terminal domain of the Nipah virus P/V protein from combined NMR and SAXS
M Schiavina, E Salladini, MG Murrali, G Tria, IC Felli, R Pierattelli, S Longhi
Scientific Reports 10 (1), 19574, 2020

Monitoring the Interaction of α‐Synuclein with Calcium Ions through Exclusively Heteronuclear Nuclear Magnetic Resonance Experiments
L Pontoriero, M Schiavina, MG Murrali, R Pierattelli, IC Felli
Angewandte Chemie 132 (42), 18696-18704, 2020

The ambivalent role of proline residues in an intrinsically disordered protein: from disorder promoters to compaction facilitators
B Mateos, C Conrad-Billroth, M Schiavina, A Beier, G Kontaxis, R Konrat, IC Felli, R Pierattelli
Journal of molecular biology 432 (9), 3093-3111, 2020

Taking simultaneous snapshots of intrinsically disordered proteins in action
M Schiavina, MG Murrali, L Pontoriero, V Sainati, R Kümmerle, W Bermel, R Pierattelli, IC Felli
Biophysical Journal 117 (1), 46-55, 2019

Cyclized NDGA modifies dynamic α-synuclein monomers preventing aggregation and toxicity
MJ Daniels, JB Nourse Jr, H Kim, V Sainati, M Schiavina, MG Murrali, B Pan, JJ Ferrie, CM Haney, R Moons…
Scientific reports 9 (1), 2937, 2019