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The TAR DNA-binding protein (TDP-43) self-assembles into prion-like aggregates considered to be the structural hallmark of amyotrophic lateral sclerosis and frontotemporal dementia. Here we use a combination of electron microscopy, X-ray fiber diffraction, FT-IR analysis and solid-state NMR spectroscopy to investigate the molecular organization of different TDP constructs, namely the full-length TDP-43 (1-414), two C-terminal fragments (TDP-35 (90-414) and TDP-16 (267-414)) and a C-terminal trun...
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Proteins require an optimal balance of conformational flexibility and stability in their native environment to ensure their biological functions. A striking example are spidroins, spider silk proteins, which are stored at extremely high concentrations in soluble form, yet undergo amyloid‐like aggregation during spinning. Here, we elucidate the stability of the highly soluble N‐terminal domain (NT) of major ampullate spidroin 1 in the E. coli cytosol as well as in inclusion bodies containing fibr...
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