Towards a microscopic picture of coacervation in elastin-like polypeptides
We aim for a comprehensive understanding of the hydrophobic collapse and the related coacervation of elastin-like polypeptides (ELPs) by combining structural and dynamical signatures using SANS (D11) and QENS (IN5), complemented by laboratory SAXS, light scattering, CD spectroscopy, and computer simulations. Using protonated and perdeuterated versions of the ELP GVG(VPGVG)42, we address the dynamical nature and conformational state of ELPs in coacervates. The studied system not only provides a model system for the hydrophobic segments of elastin which are relevant for the extraordinary mechanical properties in biology and elastin-based biomaterials. In addition, the results pave the way for future research using cellular peptides with similar phenomenology. The project is based on an established collaboration between Malmö University and the ILL (LSS group, D-Lab and theory group). The recombinant production of protonated and perdeuterated ELPs has been successfully established in the D-Lab, and sufficient material for this proposal has been expressed. The collaboration has ample expertise regarding the characterization of dynamics and structure in protein solutions and assemblies
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The recommended format for citing this dataset in a research publication is in the following format:
ROOSEN RUNGE Felix; FORSYTH Victor Trevor; HAERTLEIN Michael; KOZA Michael Marek; MATSARSKAIA Olga; MOROZOVA Tatiana; MOULIN Martine; Sarah Waldie and WEHBE Zeina. (2021). Towards a microscopic picture of coacervation in elastin-like polypeptides. Institut Laue-Langevin (ILL) doi:10.5291/ILL-DATA.8-04-929
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This data is not yet public
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