Experimental Characterization of Fuzzy Protein Assemblies: Interactions of Paramyxoviral NTAIL Domains With Their Functional Partners

Francesca Troilo, Christophe Bignon, Stefano Gianni, M. Fuxreiter, Sonia Longhi

Research output: Contribution to journalArticle

4 Citations (Scopus)


In this chapter we detail various experimental approaches to characterize the fuzziness of complexes made of the C-terminal domain of the nucleoprotein (NTAIL) from three representative paramyxoviruses and of the C-terminal X domain (XD) of the homologous phosphoprotein. We discuss the advantages, the limitations, as well as the caveats of the various methods. We describe experimental data showing that paramyxoviral NTAIL–XD complexes are characterized by a considerable amount of conformational heterogeneity. We also detail recent data that revealed that NTAIL is highly malleable, i.e., it displays a partner-mediated polymorphism. All the results suggest that NTAIL plasticity and fuzziness play a role in the coordination and regulation of the NTAIL interaction network so as to ensure efficient transcription and replication.

Original languageEnglish
JournalMethods in Enzymology
Publication statusAccepted/In press - Jan 1 2018



  • ESI-MS and IM-MS
  • Experimental assessment of fuzziness
  • Fuzzy interactions
  • Impact of fuzziness on binding
  • Kinetics
  • Mutagenesis
  • NMR
  • Protein complementation assays
  • SAXS
  • SEC
  • Site-directed spin-labeling EPR spectroscopy
  • Split-GFP reassembly

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology

Cite this