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Spectra for Lipidic folding pathway of α-Synuclein via a toxic oligomer
NMR spectra for Lipidic folding pathway of α-Synuclein via a toxic oligomer -
The clinical drug candidate anle138b binds in a cavity of lipidic α-synuclein...
This dataset includes NMR spectra raw data generated in this study, Negative stain EM micrographs for αSyn fibrils in the presence of anle138b and mass spectrometry data for the... -
A neutron study of capability of aggregation of the Abeta1-40, Abeta1-42 and ...
The aim of the proposed SANS experiment is to study the capability of aggregation, the shape and the size of aggregates of three amyloid peptides named (Abeta1-40, Abeta1-42 and... -
Neutron scattering investigation of the influence of high hydrostatic pressur...
Amyloid fibrils are highly organized filamentous structures formed by the self-assembly of polypeptides. This proposal is to study the effect of pressure on the structure of... -
Investigation of the structure of self-assembling peptide fibrils using neutr...
A consortium of several UK universities and industries has been set up, based at the National Physical Laboratory, Teddington, to investigate ¿Length-scale bridging in... -
A SANS Study on the Influence of Shear on Peptide Fibrillisation
Time-resolved SANS will be performed to investigate the effect of shear on the fibrillisation of insulin following denaturation. The rheological response will be measured...
