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.
- protein conformation
- circular dichroism
- computer simulations
- molecular dynamics
Raffaini, G., Milani, R., Ganazzoli, F., Resnati, G., & Metrangolo, P. (2016). Atomistic simulation of hydrophobin HFBII conformation in aqueousand fluorous media and at the water/vacuum interface. Journal of Molecular Graphics and Modelling, 63, 8-14. https://doi.org/10.1016/j.jmgm.2015.11.006