Highlights•Compositions of IDPs fall into distinct classes.•Compositional classes encode
preferences for distinct conformational classes.•Functions of disordered proteins are …

Intrinsically disordered proteins are ubiquitous throughout all known proteomes, playing
essential roles in all aspects of cellular and extracellular biochemistry. To understand their …

The dynamic modes and time scales sampled by intrinsically disordered proteins (IDPs)
define their function. Nuclear magnetic resonance (NMR) spin relaxation is probably the …

Amyloid formation of proteins is not only relevant for neurodegenerative diseases, but has
recently emerged as a groundbreaking approach in materials science and biotechnology …

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 …

Organic solvent nanofiltration (OSN) is regarded as a promising separation technology in
chemical and pharmaceutical industries. However, it remains a great challenge in …

The limited water solubility and bioactivity of hydrophobic phytochemicals can be improved
and preserved by encapsulation technologies. In this research, a low-cost and low-energy …

Nuclear magnetic resonance (NMR) spectroscopy is one of the most powerful experimental
approaches for investigating the conformational behaviour of intrinsically disordered …

The discovery of Intrinsically Disordered Proteins, which contain significant levels of disorder
yet perform complex biologically functions, as well as unwanted aggregation, has motivated …

Secondary structure assignment codes were built to explore the regularities associated with
the periodic motifs of proteins, such as those in backbone dihedral angles or in hydrogen …