Conditions including heating mode, time, temperature, pH, moisture and protein
concentration, shear, and the presence of alcohols, chaotropic/reducing agents, enzymes …

More than 20 human diseases, including Alzheimer's disease, Parkinson's disease, and
prion disease, originate from the deposition of misfolded proteins. These proteins, referred …

Disulfide bonds are naturally formed in more than 50% of amyloidogenic proteins, but the
exact role of disulfide bonds in protein aggregation is still not well-understood. The …

Bacillus subtilis biofilm formation relies on the assembly of a fibrous scaffold formed by the
protein TasA. TasA polymerizes into highly stable fibers with biochemical and morphological …

Amyloid fibrils are the hallmarks of neurodegenerative diseases like Alzheimer's,
Parkinson's and other proteopathies. Inhibition of fibrillation is a potential strategy to check …

The present study details the binding process of clofazimine to hen egg white lysozyme
(HEWL) using spectroscopy, dynamic light scattering, transmission electron microscopy …

Structural biology of proteins emphasises that proteins ought to have an ordered structure to
perform their biological role optimally. The over-reliance on the ordered structure of proteins …

Trehalose is a well-known protein stabilizing osmolyte. The present study has been
designed to understand the interaction of trehalose with BSA at ambient temperature …

Proteins can transform from their native state to a state having fibrillar aggregates
characterized by cross β sheet structure. The fibrillar aggregates are known as amyloid and …

Herein, we report the preparation and characterization of a new biocatalyst based on the
photo-immobilization of a lipase onto hybrid protein: sugar nanofibrils. The nanofibrils are …