Their native state is the lowest energy state

Their native state is the most disordered state (highest entropy)

Their native state is what they are trying to become

The transition to their native state has a very high and positive

Their binding to unfolded proteins is a passive, energy-free process.

All molecular chaperones are proteins themselves.

Their size ranges from monomers to large multisubunit proteins.

All are also ATPases.

They help prevent hydrophobic segments of proteins from binding to each other.

Protein folding diseases usually occur when beta-sheets misfold and precipitate into alpha-helices.

Chaperones are proteins that help other proteins fold properly.

The hydrophobic collapse causes formation of protein secondary, tertiary, and native state structure in that order.

DnaJ and DnaK are chaperones in E. coli that coat the unfolded protein to prevent aggregation.