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Issue 27, 2016
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Extending the essential dynamics analysis to investigate molecular properties: application to the redox potential of proteins

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Abstract

Here, a methodology is proposed to investigate the collective fluctuation modes of an arbitrary set of observables, maximally contributing to the fluctuation of another functionally relevant observable. The methodology, based on the analysis of fully classical molecular dynamics (MD) simulations, exploits the essential dynamics (ED) method, originally developed to analyse the collective motions in proteins. We apply this methodology to identify the residues that are more relevant for determining the reduction potential (E0) of a redox-active protein. To this aim, the fluctuation modes of the single-residue electrostatic potentials mostly contributing to the fluctuations of the total electrostatic potential (the main determinant of E0) are investigated for wild-type azurin and two of its mutants with a higher E0. By comparing the results here obtained with a previous study on the same systems [Zanetti-Polzi et al., Org. Biomol. Chem., 2015, 13, 11003] we show that the proposed methodology is able to identify the key sites that determine E0. This information can be used for a general deeper understanding of the molecular mechanisms on the basis of the redox properties of the proteins under investigation, as well as for the rational design of mutants with a higher or lower E0. From the results of the present analysis we propose a new azurin mutant that, according to our calculations, shows a further increase of E0.

Graphical abstract: Extending the essential dynamics analysis to investigate molecular properties: application to the redox potential of proteins

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Supplementary files

Article information


Submitted
18 May 2016
Accepted
07 Jun 2016
First published
07 Jun 2016

Phys. Chem. Chem. Phys., 2016,18, 18450-18459
Article type
Paper

Extending the essential dynamics analysis to investigate molecular properties: application to the redox potential of proteins

L. Zanetti-Polzi, S. Corni, I. Daidone and A. Amadei, Phys. Chem. Chem. Phys., 2016, 18, 18450
DOI: 10.1039/C6CP03394F

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