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- W2894934111 endingPage "192" @default.
- W2894934111 startingPage "137" @default.
- W2894934111 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." @default.
- W2894934111 created "2018-10-12" @default.
- W2894934111 creator A5002870553 @default.
- W2894934111 creator A5008132760 @default.
- W2894934111 creator A5012700817 @default.
- W2894934111 creator A5013000080 @default.
- W2894934111 creator A5074212421 @default.
- W2894934111 date "2018-01-01" @default.
- W2894934111 modified "2023-10-04" @default.
- W2894934111 title "Experimental Characterization of Fuzzy Protein Assemblies: Interactions of Paramyxoviral NTAIL Domains With Their Functional Partners" @default.
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