Intrinsically disordered proteins (IDPs) do not attain a stable secondary or tertiary structure and rapidly change their conformation, making structure prediction particularly challenging.

The intrinsically disordered proteins (IDPs) do not attain a stable secondary or tertiary structure and rapidly change their conformation, making structure prediction particularly challenging.

Protein folding is the process by which proteins achieve their mature functional (native) tertiary structure, and often begins co-translationally. Protein folding requires chaperones and often ...

Enzymes found in landfills around the world may be able to break down plastic waste. Some 11 billion metric tons of plastic ...

Intrinsically disordered proteins are isolated polypeptide chains with no stable tertiary structure under physiological conditions in vitro. They remain functional despite the lack of a well ...

The intrinsically disordered proteins (IDPs) do not attain a stable secondary or tertiary structure and rapidly change their ...

These are precision polymers, and they form primary, secondary, and tertiary structures ... Amyloid fibrils are a secondary structure of protein, a class of protein aggregate.

The Supporting Information is available free of charge at https://pubs.acs.org/doi/10.1021/acs.biomac.4c00991. BSA structure analysis under different shear rates ...

Haemolytic disease of the fetus and newborn (HDFN) occurs when there is transplacental passage of maternal immunoglobulin G ...

Innovations in food science and immunology are unlocking a future where allergy-free living is within reach.