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Maturation-dependent changes in the size, structure and seeding capacity of Aβ42 amyloid fibrils - Communications Biology

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Maturation-dependent changes in the size, structure and seeding capacity of Aβ42 amyloid fibrils - Communications Biology

Many proteins self-assemble to form amyloid fibrils, which are highly organized structures stabilized by a characteristic cross-β network of hydrogen bonds. This process underlies a variety of human diseases and can be exploited to develop versatile functional biomaterials. Thus, protein self-assembly has been widely studied to shed light on the properties of fibrils and their intermediates. A still

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Maturation-dependent changes in the size, structure and seeding capacity of Aβ42 amyloid fibrils - Communications Biology

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Maturation-dependent changes in the size, structure and seeding capacity of Aβ42 amyloid fibrils - Communications Biology

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