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    Free energy of binding of coiled-coil complexes with different electrostatic environments: the influence of force field polarisation and capping

    213177_213177.pdf (1.630Mb)
    Access Status
    Open access
    Authors
    Zhuo, Z.
    Guo, L.
    Mancera, Ricardo
    Date
    2014
    Type
    Journal Article
    
    Metadata
    Show full item record
    Citation
    Zhuo, Z. and Guo, L. and Mancera, R. 2014. Free energy of binding of coiled-coil complexes with different electrostatic environments: the influence of force field polarisation and capping. Natural Products and Bioprospecting. 4: pp. 285-295.
    Source Title
    Natural Products and Bioprospecting
    DOI
    10.1007/s13659-014-0036-0
    ISSN
    21922209
    School
    School of Biomedical Sciences
    Remarks

    This article is published under the Open Access publishing model and distributed under the terms of the Creative Commons License http://creativecommons.org/licenses/by/4.0/ Please refer to the licence to obtain terms for any further reuse or distribution of this work.

    URI
    http://hdl.handle.net/20.500.11937/12472
    Collection
    • Curtin Research Publications
    Abstract

    Coiled-coils are well known protein–protein interaction motifs, with the leucine zipper region of activator protein-1 (AP-1) consisting of the c-Jun and c-Fos proteins being a typical example. Molecular dynamics (MD) simulations using the MM/GBSA method have been used to predict the free energy of interaction of these proteins. The influence of force field polarisation and capping on the predicted free energy of binding of complexes with different electrostatic environments (net charge) were investigated. Although both force field polarisation and peptide capping are important for the prediction of the absolute free energy of binding, peptide capping has the largest influence on the predicted free energy of binding. Polarisable simulations appear better suited to determine structural properties of the complexes of these proteins while non-polarisable simulations seem to give better predictions of the associated free energies of binding

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