0000000001335532
AUTHOR
Leone, Maurizio
THz spectroscopy study of amyloid fibrils
In suitable conditions proteins can modify their native conformation and associate to form aggregates with different morphologies in dependence on the external physico-chemical conditions. This phenomenon, one of the most challenging in life sciences, is associated with widely diffused pathologies such as Alzheimer’s, Parkinson’s and Creutzfeldt-Jacob’s diseases. Of particular relevance are ordered elongated aggregates with highly organized patterns of hydrogen-bonds, known as amyloid fibrils. While much biological and structural information are available about amyloids, and in spite of the fundamental paradigm of structure-dynamics-function relation in proteins, much less is known about th…
Insights into amyloid fibrils dynamics from neutron scattering
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