Atomistic simulation of hydrophobin HFBII conformation in aqueousand fluorous media and at the water/vacuum interface

Giuseppina Raffaini (Corresponding Author), Roberto Milani (Corresponding Author), Fabio Ganazzoli, Giuseppe Resnati, Pierangelo Metrangolo (Corresponding Author)

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    Abstract

    Hydrophobins are proteins of interest for numerous applications thanks to their unique conformationaland surface properties and their ability to self-assemble at interfaces. Here we report fully atomisticmolecular mechanics and molecular dynamics results together with circular dichroism experimentaldata, aimed to study the conformational properties of the hydrophobin HFBII in a fluorinated solvent incomparison with a water solution and/or at an aqueous/vacuum interface. Both the atomistic simulationsand the circular dichroism data show the remarkable structural stability of HFBII at all scales in all theseenvironments, with no significant structural change, although a small cavity is formed in the fluorinatedsolvent. The combination of theoretical calculations and circular dichroism data can describe in detailthe protein conformation and flexibility in different solvents and/or at an interface, and constitutes a firststep towards the study of their self-assembly.
    Original languageEnglish
    Pages (from-to)8-14
    JournalJournal of Molecular Graphics and Modelling
    Volume63
    DOIs
    Publication statusPublished - 2016
    MoE publication typeA1 Journal article-refereed

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    Keywords

    • hydrophobin
    • protein conformation
    • circular dichroism
    • computer simulations
    • molecular dynamics

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