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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Veröffentlicht in:J Biol Chem
Hauptverfasser: Karlsson, Elin, Paissoni, Cristina, Erkelens, Amanda M., Tehranizadeh, Zeinab A., Sorgenfrei, Frieda A., Andersson, Eva, Ye, Weihua, Camilloni, Carlo, Jemth, Per
Format: Artigo
Sprache:Inglês
Veröffentlicht: American Society for Biochemistry and Molecular Biology 2020
Schlagworte:
Protein Structure and Folding
Online Zugang:https://ncbi.nlm.nih.gov/pmc/articles/PMC7762952/
https://ncbi.nlm.nih.gov/pubmed/33454008
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1074/jbc.RA120.015645
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