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Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy
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Formation kinetics and structural features of Beta-amyloid aggregates by sedimented solute NMR

Ivano Bertini1, Gianluca Gallo, Magdalena Korsak

  • 1Magnetic Resonance Center (CERM), University of Florence, Via L. Sacconi 6, 50019 Sesto Fiorentino (Italy); Giotto Biotech, Via Madonna del Piano 6, 50019 Sesto Fiorentino (Italy); Fondazione Farmacogenomica FiorGen onlus Via L. Sacconi 6, 50019 Sesto Fiorentino (Italy).

Chembiochem : a European Journal of Chemical Biology
|July 4, 2013
PubMed

Keywords:
centrifugationkineticsoligomerizationsedimentationsolid-state NMR spectroscopy

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Amyloid Fibrils03:03

Amyloid Fibrils

Amyloid fibrils are aggregates of misfolded proteins.  Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils. 
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Amyloid Fibrils

Amyloid fibrils are aggregates of misfolded proteins.  Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils. 
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