Mapping the transition state for a binding reaction between ancient intrinsically disordered proteins

Intrinsically disordered protein domains often have multiple binding partners. It is plausible that the strength of pairing with specific partners evolves from an initial low affinity to a higher affinity. However, little is known about the molecular changes in the binding mechanism that would facil...

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Detalles Bibliográficos
Autores principales: Karlsson, Elin, Paissoni, Cristina, Erkelens, Amanda M., Tehranizadeh, Zeinab A., Sorgenfrei, Frieda A., Andersson, Eva, Ye, Weihua, Camilloni, Carlo, Jemth, Per
Formato: Online Artículo Texto
Lenguaje:English
Publicado: American Society for Biochemistry and Molecular Biology 2020
Materias:
Protein Structure and Folding
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7762952/
https://www.ncbi.nlm.nih.gov/pubmed/33454008
http://dx.doi.org/10.1074/jbc.RA120.015645

Internet

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7762952/
https://www.ncbi.nlm.nih.gov/pubmed/33454008
http://dx.doi.org/10.1074/jbc.RA120.015645

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