Data for ion and seed dependent fibril assembly of a spidroin core domain.

Martin Humenik, Andrew M Smith, Sina Arndt, Thomas Scheibel

    Research output: Contribution to journalArticlepeer-review

    Abstract

    This data article includes size exclusion chromatography data of soluble eADF4(C16), an engineered spider silk variant based on the core domain sequence of the natural dragline silk protein ADF4 of Araneus diadematus, in combination with light scattering; the protein is monomeric before assembly. The assembled mature fibrils were visualized by transmission electron microscopy (TEM) and atomic force microscopy (AFM). Sonicated fibrils were used as seeds to by-pass the nucleation lag phase in eADF4(C16) assembly. We also provide data on the sedimentation kinetics of spider silk in the presence of different NaCl concentrations revealing very slow protein aggregation in comparison to the fast assembly triggered by phosphate ions published previously [1]. Experiments in the Data article represent supporting material for our work published recently [1], which described the assembly mechanism of recombinant eADF4(C16) fibrils.
    Original languageEnglish
    Pages (from-to)571-6
    Number of pages6
    JournalData in Brief
    Volume4
    Publication statusPublished - 2015

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