Skip to Main Content (Press Enter)

Logo CNR
  • ×
  • Home
  • People
  • Outputs
  • Organizations
  • Expertise & Skills

UNI-FIND
Logo CNR

|

UNI-FIND

cnr.it
  • ×
  • Home
  • People
  • Outputs
  • Organizations
  • Expertise & Skills
  1. Outputs

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

Academic Article
Publication Date:
2018
abstract:
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.
Iris type:
01.01 Articolo in rivista
Keywords:
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
List of contributors:
Gianni, Stefano
Handle:
https://iris.cnr.it/handle/20.500.14243/356787
Published in:
METHODS IN ENZYMOLOGY
Series
  • Overview

Overview

URL

http://www.scopus.com/inward/record.url?eid=2-s2.0-85054544623&partnerID=q2rCbXpz
  • Use of cookies

Powered by VIVO | Designed by Cineca | 26.5.0.0 | Sorgente dati: PREPROD (Ribaltamento disabilitato)