Chaperone proteins, often referred to as molecular chaperones, are a diverse group of proteins that assist in the folding and maintenance of other proteins within the cell. They ensure that newly synthesized proteins attain their proper three-dimensional structures and function correctly. Key families of chaperone proteins include heat shock proteins (HSPs), GroEL/GroES in bacteria, and calnexin/calreticulin in the endoplasmic reticulum.
