清华本科课件《生物化学》Ch4-II 4273067.pptVIP

* FIGURE 4-30a * FIGURE 4-30b Chaperonins in protein folding. (b) Surface and cut-away images of the GroEL/GroES complex (PDB ID 1AON). The cut-away (right) illustrates the large interior space within which other proteins are bound. * FIGURE 4-31a Formation of disease-causing amyloid fibrils. * FIGURE 4-31b Formation of disease-causing amyloid fibrils. (b) The amyloid-β peptide, which plays a major role in Alzheimer’s disease, is derived from a larger transmembrane protein called amyloid-β precursor protein or APP. This protein is found in most human tissues. When it is part of the larger protein, the peptide is composed of two α-helical segments spanning the membrane. When the external and internal domains (each of which have independent functions) are cleaved off by dedicated proteases, the remaining and relatively unstable amyloid-β peptide leaves the membrane and loses its α-helical structure. * FIGURE 4-31c Formation of disease-causing amyloid fibrils. It can then assemble slowly into amyloid fibrils (c), which contribute to the characteristic plaques on the exterior of nervous tissue in people with Alzheimer’s. Amyloid is rich in β-sheet structure, with the β strands arranged perpendicular to the axis of the amyloid fibril. In amyloid-β peptide, the structure takes the form of an extended two-layer parallel β sheet. Others may take the form of left-handed β-helices (see Figure 4-21). * BOX 4-6 FIGURE 1 Stained section of cerebral cortex from autopsy of a patient with Creutzfeldt-Jakob disease shows spongiform (vacuolar) degeneration, the most characteristic neurohistological feature. The yellowish vacuoles are intracellular and occur mostly in pre- and postsynaptic processes of neurons. The vacuoles in this section vary in diameter from 20 to 100 μm. * BOX 4-6 FIGURE 2 Structure of the globular domain of human PrP in monomeric (left) and dimeric (right) forms. The second subunit is gray to highlight the dramatic conformational change in the green α helix (now