Mechanism-Dependent Modulation of Ultrafast Interfacial Water Dynamics in Intrinsically Disordered Protein Complexes

Overview

Journal Angew Chem Int Ed Engl

Specialty Chemistry

Date 2019 Feb 1

PMID 30703278

Citations 6

Authors

Aritra Chowdhury

Sergey A Kovalenko

Iker Valle Aramburu

Piau Siong Tan

Nikolaus P Ernsting

Edward A Lemke

Affiliations

Soon will be listed here.

Abstract

The recognition of intrinsically disordered proteins (IDPs) is highly dependent on dynamics owing to the lack of structure. Here we studied the interplay between dynamics and molecular recognition in IDPs with a combination of time-resolving tools on timescales ranging from femtoseconds to nanoseconds. We interrogated conformational dynamics and surface water dynamics and its attenuation upon partner binding using two IDPs, IBB and Nup153FG, both of central relevance to the nucleocytoplasmic transport machinery. These proteins bind the same nuclear transport receptor (Importinβ) with drastically different binding mechanisms, coupled folding-binding and fuzzy complex formation, respectively. Solvent fluctuations in the dynamic interface of the Nup153FG-Importinβ fuzzy complex were largely unperturbed and slightly accelerated relative to the unbound state. In the IBB-Importinβ complex, on the other hand, substantial relative slowdown of water dynamics was seen in a more rigid interface. These results show a correlation between interfacial water dynamics and the plasticity of IDP complexes, implicating functional relevance for such differential modulation in cellular processes, including nuclear transport.

Citing Articles

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Extreme dynamics in a biomolecular condensate.

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The origin and impact of bound water around intrinsically disordered proteins.

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