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For quite rigid fibrils where the analyzable length is lower than the persistence length of the fibril, the following equation (derived from the worm-like chain model5 for a polymer chain that is free to move in 2 dimensions) was used to derive the persistence length PL:
We generated and analyzed amyloid fibrils of wild-type (W) mouse prion protein PrP23-231 as well as three mutants:
Recently, attention has been given to the molecular packing of collagen molecules into microfibrils (5) and their self-organization into larger fibrils.
Fourier transform infrared spectroscopy and circular dichroism showed that this conversion leads to a substantial change in the secondary structure of the prion protein.3 While PrPC has a high α-helical content (42%) and only a few residues in βsheets (3%), PrPSc has a less pronounced α-helical content (30%) and is much richer in β-sheets (43%), which is consistent with its ability to form insoluble amyloid fibrils and its partial protease resistance.
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Lamour GJPC 2011 55%
Nevertheless, collagen fibrils are supposed to provide a higher nanoroughness (i.e., vertical variations of a surface at the nanometer scale) than both PLL and PLO.
Hydrogen bonds form between adjacent chains, creating very strong cellulose fibrils