Kinetic response of a photoperturbed allosteric protein.

[Full text]653/1460[Suppl. Mat.]

Kinetic response of a photoperturbed allosteric protein.

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Kinetic response of a photoperturbed allosteric protein.

Proc Natl Acad Sci U S A. 2013 Jul 16;110(29):11725-30

Authors: Buchli B, Waldauer SA, Walser R, Donten ML, Pfister R, Blöchliger N, Steiner S, Caflisch A, Zerbe O, Hamm P

Abstract
By covalently linking an azobenzene photoswitch across the binding groove of a PDZ domain, a conformational transition, similar to the one occurring upon ligand binding to the unmodified domain, can be initiated on a picosecond timescale by a laser pulse. The protein structures have been characterized in the two photoswitch states through NMR spectroscopy and the transition between them through ultrafast IR spectroscopy and molecular dynamics simulations. The binding groove opens on a 100-ns timescale in a highly nonexponential manner, and the molecular dynamics simulations suggest that the process is governed by the rearrangement of the water network on the protein surface. We propose this rearrangement of the water network to be another possible mechanism of allostery.

PMID: 23818626 [PubMed - indexed for MEDLINE]

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