Enthalpy–Entropy Compensation in the Promiscuous Interaction of an Intrinsically Disordered Protein with Homologous Protein Partners

Enthalpy–Entropy Compensation in the Promiscuous Interaction of an Intrinsically Disordered Protein with Homologous Protein Partners

Intrinsically disordered proteins (IDPs) can engage in promiscuous interactions with their protein targets; however, it is not clear how this feature is encoded in the primary sequence of the IDPs and to what extent the surface properties and the shape of the binding cavity dictate the binding mode...

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Bibliographic Details
Main Authors: Jaka Kragelj, Thibault Orand, Elise Delaforge, Laura Tengo, Martin Blackledge, Andrés Palencia, Malene Ringkjøbing Jensen
Format: Article
Language:English
Published: MDPI AG 2021-08-01
Series:Biomolecules
Subjects:
NMR spectroscopy
isothermal titration calorimetry
intrinsically disordered protein (IDP)
mitogen-activated protein kinase (MAPK)
enthalpy–entropy compensation
folding-upon-binding
Online Access:https://www.mdpi.com/2218-273X/11/8/1204

Internet

https://www.mdpi.com/2218-273X/11/8/1204

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