Protein folding

Protein folding is the process and the pathway that proteins take to transform themselves from the unfolded state to the compact, or native state[?]. Folding is a self-directed activity, but it relies on the physics of the solvent - water. Often, the folding of a protein is assisted by a chaperone or heat shock protein[?].

Proteins that are not folded are said to be denatured. Denatured proteins lack secondary structure, in general having only a random coil[?] secondary configuration. There is an intermediate state in the path from denatured to folded, called the molten globule, that is important, as it can be easy, in de novo protein design[?], to confuse a molten globule with a native protein.

Proteins, especially enzymes, are fully functional only when folded correctly. Incorrect folding can lead to nonfunctional proteins, or worse, turn them into pathogens, as is the case with prions which cause BSE.

The determination of the actual folding of a protein is a lengthy and complicated process, involving methods like X-ray crystallography and NMR. In bioinformatics, one of the major areas of interest is the prediction of the correct protein folding from the amino acid sequence of the protein alone.

Recently a distributed computing application, folding@home, has been used to simulate protein folding.