Some proteins termed as RNA chaperone are thought to assist in RNA folding by preventing misfolding or by resolving misfolded RNA.

1, Identification of the RNA chaperone activity of human tumornecrosis factor alpha in vitro.

Effect of ATP on molecular chaperone function and conformation of α-crystallin;

Change of molecular chaperone activity of high-molecular-weight alpha-crystallin in age-related cataract;

Effects of fructose 6-phosphate and ribose on molecular chaperone activity of α-crystallin;

They work as chaperones participating in the folding and unfolding,assembly of multisubunit complexes, transportation and degradation of proteins and play an important role in biochemical function of proteins.

The properly folding of most heterologous proteins need the helper molecular chaperones.

Heat shock proteins (HSPs) are molecular chaperones that are increased by various environmental stresses (such as hazardous chemical , ionizing radiation, hyperthermia and oxidation etc).

Quality control over protein structure and function depends on the presence of molecular chaperones and proteases, which prevent aggregation.

Now, there were several studies about it, such as presequences, processing of precursor proteins, function of molecular chaperones and sorting of mitochondria and plastids(or chloroplasts).

The Effect of Over-expression of Chaperones on the Secretion and the Solubility of Proteins*;

Aim In an effort to confirm the effects of NB on Bcr-Abl expressing HL-60/Bcr-Abl cells,and the relationship between these effects and the molecular chaperone functions of heat shock protein 90(Hsp90).

The term "molecular chaperone" was originally used to describe a class of biomolecules,which mediate interactions between nuclear acids and proteins in the nucleus.