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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Ngā kaituhi matua:	Jaka Kragelj, Thibault Orand, Elise Delaforge, Laura Tengo, Martin Blackledge, Andrés Palencia, Malene Ringkjøbing Jensen
Hōputu:	Artigo
Reo:	Inglês
I whakaputaina:	MDPI AG 2021-08-01
Rangatū:	Biomolecules
Ngā marau:	NMR spectroscopy isothermal titration calorimetry intrinsically disordered protein (IDP) mitogen-activated protein kinase (MAPK) enthalpy–entropy compensation folding-upon-binding
Urunga tuihono:	https://www.mdpi.com/2218-273X/11/8/1204
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