Secondary Structure Assignment of Amyloid-β Peptide Using Chemical Shifts

The distinct conformational dependence of chemical shifts caused by R-helices and β-sheets renders NMR chemical shift analysis a powerful tool for the structural determination of proteins. However, the time scale of NMR experiments can make a secondary structure assignment of highly flexible peptides or proteins, which may be converting between conformational substates, problematic. For instance the amyloid-β monomer, according to NMR chemical shifts, adopts a predominately random coil struc- ture in aqueous solution (with

Secondary Structure Assignment of Amyloid-β Peptide Using Chemical Shifts

Structure determination of an amorphous drug through large-scale NMR predictions

Assessment of transferable forcefields for protein simulations attests improved description of disordered states and secondary structure propensities, and hints at multi-protein systems as the next challenge for optimization

Molecular dissection of amyloid disaggregation by human HSP70

Molecular dissection of amyloid disaggregation by human HSP70

Assessment of transferable forcefields for protein simulations attests improved description of disordered states and secondary structure propensities, and hints at multi-protein systems as the next challenge for optimization

Structure determination of an amorphous drug through large-scale NMR predictions