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Updated: Mar 29, 2026

Multiscale Sampling of a Heterogeneous Water/Metal Catalyst Interface using Density Functional Theory and Force-Field Molecular Dynamics
Published on: April 12, 2019
Atomistic simulation of hydrophobin HFBII conformation in aqueous and fluorous media and at the water/vacuum
Giuseppina Raffaini1, Roberto Milani2, Fabio Ganazzoli1
1Dipartimento di Chimica, Materiali ed Ingegneria Chimica "Giulio Natta", Politecnico di Milano, Via L. Mancinelli 7, 20131 Milano, Italy; Unità Politecnico, INSTM, Piazza Leonardo da Vinci 32, 20133 Milano, Italy.
Abstract:
Hydrophobins are proteins of interest for numerous applications thanks to their unique conformational and surface properties and their ability to self-assemble at interfaces. Here we report fully atomistic molecular mechanics and molecular dynamics results together with circular dichroism experimental data, aimed to study the conformational properties of the hydrophobin HFBII in a fluorinated solvent in comparison with a water solution and/or at an aqueous/vacuum interface. Both the atomistic simulations and the circular dichroism data show the remarkable structural stability of HFBII at all scales in all these environments, with no significant structural change, although a small cavity is formed in the fluorinated solvent. The combination of theoretical calculations and circular dichroism data can describe in detail the protein conformation and flexibility in different solvents and/or at an interface, and constitutes a first step towards the study of their self-assembly.
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