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 journalArticleScientificpeer-review

    6 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 languageEnglish
    Pages (from-to)8-14
    JournalJournal of Molecular Graphics and Modelling
    Volume63
    DOIs
    Publication statusPublished - 2016
    MoE publication typeA1 Journal article-refereed

    Fingerprint

    Dichroism
    dichroism
    Conformations
    Vacuum
    vacuum
    Water
    Self assembly
    water
    proteins
    Surface properties
    Proteins
    Molecular dynamics
    Mechanics
    simulation
    structural stability
    surface properties
    self assembly
    flexibility
    molecular dynamics
    cavities

    Keywords

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

    Cite this

    Raffaini, Giuseppina ; Milani, Roberto ; Ganazzoli, Fabio ; Resnati, Giuseppe ; Metrangolo, Pierangelo. / Atomistic simulation of hydrophobin HFBII conformation in aqueousand fluorous media and at the water/vacuum interface. In: Journal of Molecular Graphics and Modelling. 2016 ; Vol. 63. pp. 8-14.
    @article{538c466052a940eab8784719c6ef91fb,
    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",

    }

    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; Resnati, Giuseppe; Metrangolo, Pierangelo (Corresponding Author).

    In: Journal of Molecular Graphics and Modelling, Vol. 63, 2016, p. 8-14.

    Research output: Contribution to journalArticleScientificpeer-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

    VL - 63

    SP - 8

    EP - 14

    JO - Journal of Molecular Graphics and Modelling

    JF - Journal of Molecular Graphics and Modelling

    SN - 1093-3263

    ER -