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

Giuseppina Raffaini; Roberto Milani; Fabio Ganazzoli; Giuseppe Resnati; Pierangelo Metrangolo

doi:10.1016/j.jmgm.2015.11.006

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)

Research output: Contribution to journal › Article › Scientific › peer-review

11 Citations (Scopus)

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 language	English
Pages (from-to)	8-14
Journal	Journal of Molecular Graphics and Modelling
Volume	63
DOIs	https://doi.org/10.1016/j.jmgm.2015.11.006
Publication status	Published - 2016
MoE publication type	A1 Journal article-refereed

Keywords

hydrophobin
protein conformation
circular dichroism
computer simulations
molecular dynamics

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10.1016/j.jmgm.2015.11.006

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

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.",

keywords = "hydrophobin, protein conformation, circular dichroism, computer simulations, molecular dynamics",

author = "Giuseppina Raffaini and Roberto Milani and Fabio Ganazzoli and Giuseppe Resnati and Pierangelo Metrangolo",

note = "Project code: 101066 Project code: 100495 ",

year = "2016",

doi = "10.1016/j.jmgm.2015.11.006",

language = "English",

volume = "63",

pages = "8--14",

journal = "Journal of Molecular Graphics and Modelling",

issn = "1093-3263",

publisher = "Elsevier Inc.",

}

Atomistic simulation of hydrophobin HFBII conformation in aqueousand fluorous media and at the water/vacuum interface. / Raffaini, Giuseppina (Corresponding Author); Milani, Roberto (Corresponding Author); Ganazzoli, Fabio et al.
In: Journal of Molecular Graphics and Modelling, Vol. 63, 2016, p. 8-14.

Research output: Contribution to journal › Article › Scientific › peer-review

TY - JOUR

T1 - Atomistic simulation of hydrophobin HFBII conformation in aqueousand fluorous media and at the water/vacuum interface

AU - Raffaini, Giuseppina

AU - Milani, Roberto

AU - Ganazzoli, Fabio

AU - Resnati, Giuseppe

AU - Metrangolo, Pierangelo

N1 - Project code: 101066 Project code: 100495

PY - 2016

Y1 - 2016

N2 - 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.

AB - 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.

KW - hydrophobin

KW - protein conformation

KW - circular dichroism

KW - computer simulations

KW - molecular dynamics

U2 - 10.1016/j.jmgm.2015.11.006

DO - 10.1016/j.jmgm.2015.11.006

M3 - Article

SN - 1093-3263

VL - 63

SP - 8

EP - 14

JO - Journal of Molecular Graphics and Modelling

JF - Journal of Molecular Graphics and Modelling

ER -

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

Abstract

Keywords

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