Amyloid beta (Aβ or Abeta) is a peptide of 36–43 amino acids that is processed from the Amyloid precursor protein. While best known as a component of amyloid plaques in association with Alzheimer's disease, evidence has been found that Aβ is a highly multifunctional peptide with significant non-pathological activity.[1] Aβ is the main component of deposits found in the brains of patients with Alzheimer's disease
Beta Amyloid Fibrils Formation Structure & Growth ~ Top 100 Papers on Amyloid Beta Fibrils Formation Structure & Growth~
Beta Amyloid Fibrils Formation Structure & Growth ~ Top 100 Papers on Amyloid Beta Fibrils Formation Structure & Growth~
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The simulation: fibrils are thought to be symmetric assemblies, which means that they are formed by stacking together many identical copies of a protein or peptide. What you see on your screen are 12 copies of the Abeta(10-40) sequence (our collaborators tell us that residues 1-9 are likely to be disordered and outside the core of the fibril). There will be a low-resolution simulation (no sidechains visible, lots of movement), followed by a high-resolution refinement (sidechains visible in the left panel, simulation appears to go much more slowly). Not all low-resolution trajectories will go on to high-res refinement -- we are filtering for conformations which satisfy the experimental constraints.
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Brenda Watt, Guillaume van Niel, Douglas M. Fowler, Ilse Hurbain, Kelvin C. Luk, Steven E. Stayrook, Mark A. Lemmon, Graça Raposo, James Shorter, Jeffery W. Kelly, Michael S. Marks
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