The three-dimensional structures of lysozyme (Protein Data Bank code 1LYY ... chains converge into a cross-beta super-secondary structure that has been well characterized by x-ray diffraction ...

Researchers found that peristaltic pump flow mechanically breaks supersaturation to induce amyloid formation by hen egg white lysozyme, a-synuclein, amyloid b 1-40, and b2-microglobulin.

So Landau plans to use the newly acquired structure to design inhibitors of the amyloid as potential antibiotics. Inhibiting formation of the PSMα3 amyloid could provide a way to decrease ...

Structure of hnRNPDL-2 amyloid fibres obtained by cryoEM at 2.5 A resolution. The upper part shows the organisation of the protein with two nucleic acid binding domains in pink and a low ...

To address this, the researchers ran a model amyloid-forming protein, hen egg white lysozyme, through a peristaltic pump similar to those used for dialysis. They then used fluorescence detection ...

New research suggests that Alzheimer’s disease may trigger increased expression of an enzyme called lysozyme, which attempts to counteract amyloid build-up in the brain. New research suggests ...

For their new study, the scientists investigated the reasons why TAP01_04 was able to target the soluble amyloid beta so specifically, by solving its crystal structure. This revealed that part of ...

Amyloid fibrils contain a core structure of polypeptide chains arranged in antiparallel β-pleated sheets lying with their long axes perpendicular to the long axis of the fibril (Figure 2A).

Yuji Goto, lead author of the study To address this, the researchers ran a model amyloid-forming protein, hen egg white lysozyme, through a peristaltic pump similar to those used for dialysis.