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Adhesive water networks facilitate binding of protein interfaces.

Abstract：

:Water structure has an essential role in biological assembly. Hydrophobic dewetting has been documented as a general mechanism for the assembly of hydrophobic surfaces; however, the association mechanism of hydrophilic interfaces remains mysterious and cannot be explained by simple continuum water models that ignore the solvent structure. Here we study the association of two hydrophilic proteins using unbiased extensive molecular dynamics simulations that reproducibly recovered the native bound complex. The water in the interfacial gap forms an adhesive hydrogen-bond network between the interfaces stabilizing early intermediates before native contacts are formed. Furthermore, the interfacial gap solvent showed a reduced dielectric shielding up to distances of few nanometres during the diffusive phase. The interfacial gap solvent generates an anisotropic dielectric shielding with a strongly preferred directionality for the electrostatic interactions along the association direction.

journal_name

Nat Commun

journal_title

Nature communications

authors

Ahmad M,Gu W,Geyer T,Helms V

doi

10.1038/ncomms1258

subject

Has Abstract

pub_date

2011-03-29 00:00:00

pages

261

issn

2041-1723

pii

ncomms1258

journal_volume

2

pub_type

杂志文章

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