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

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 ...

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

Meenakshi is the Editor-in-Chief at The Scientist. Her diverse science communication experience includes journalism, podcasting, and content strategy. Meenakshi earned her PhD in biophysics from the ...

Proteins are essential macromolecules that play a crucial role in virtually all biological processes. They are the building blocks of life, performing a wide range of functions within organisms, from ...

tRNAs have a distinct cloverleaf secondary structure and an L-shaped tertiary structure. The cloverleaf structure is formed by the folding of the single-stranded tRNA molecule, which is typically ...

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 ...