Localised semicrystalline phases of MaSp1 proteins show high sensitivity to overshearing in β-sheet nanocrystals

Erly Sintya, Parvez Alam

    Research output: Contribution to journalArticleScientificpeer-review

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    Abstract

    We consider the effects of β-sheet over-shearing on the development of semi-crystallinity in clusters of MaSp1 spider dragline silk proteins. Using molecular dynamics methods, we find that the extent of crystalline matter in the localised region of an over-sheared nanocrystal can in fact increase through over-shearing β-sheets. This is due to both; the influence of β-sheets on surrounding amorphous matter and the influence of amorphous matter in destabilising β-sheets at their interfaces. In both cases the result is the development of increased molecular order. Beyond a critical distance of over-shearing, crystallinity decreases due to a decrease in the stability of both over-sheared β-sheets and amorphous matter. Crystallinity of a system as a function of overshearing of β-sheets follows a Gaussian form. Larger stacks of overshearing β-sheets are energetically more stable than smaller stacks and are consequently able to develop the highest levels of crystallinity within the model systems. The elastic moduli computed herein indicate that the most crystalline oversheared systems are heightened in stiffness through overshearing, though there is concurrently a decrease in extensibility.
    Original languageUndefined/Unknown
    Pages (from-to)1006–1011
    JournalInternational Journal of Biological Macromolecules
    Volume92
    DOIs
    Publication statusPublished - 2016
    MoE publication typeA1 Journal article-refereed

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