Médoune Sarr

TL;DR: The mechanisms controlling the conversion of spider silk proteins into insoluble fibres, which happens in a fraction of a second and in a defined region of the silk glands, are still unresolved.

TL;DR: This work hypothesizes that fusion to NT could similarly solubilize non-spidroin proteins, and design a charge-reversed mutant (NT*) that is pH insensitive, stabilized and hypersoluble compared to wild-type NT, and enables transmembrane peptide purification to homogeneity without chromatography.

TL;DR: A designed variant of NT from Nephila clavipes flagelliform spidroin, which in nature allows production and storage of β-hairpin repeat segments, gives exceptionally high yields of different human Aβ variants as a solubility tag, which enables efficient production of target peptides also in minimal medium.

TL;DR: Whether fusion to NT* can prevent amyloid fibril formation and enable controlled aggregation for experimental studies is investigated and the ability of NT* to prevent premature aggregation and to enable structural studies of prefibrillar states may facilitate investigation of proteins involved inAmyloid diseases.

TL;DR: It is demonstrated how a peripheral membrane protein uses lipids to modulate its structure in a similar manner as integral membrane proteins.