Las chaperonas moleculares o proteínas de choque térmico, son una amplia familia de
proteínas sin relación que han sido caracterizadas principalmente por sus funciones vitales …

Abstract The chaperonin 60 (Cpn60) is present in all three kingdoms of life and is one of the
most conserved proteins in living organisms. The Escherichia coli Cpn60 (GroEL) is the best …

GroEL is a chaperonin that helps other proteins fold correctly. However, alternative activities,
such as acting as an insect toxin, have also been discovered. This work evaluates the …

Las proteínas son moléculas de elevada importancia en los seres vivos. Impresionante
resulta la vasta cantidad de funciones que cumplen dentro y fuera de estos. Una de las …

GroEL is a multifunctional protein belonging to the conspicuous family of chaperones active
in prokaryotic and eukaryotic cells. GroEL of Escherichia coli is a heat shock-like protein …

The heat-shock protein GroEL is a double-ring–structured chaperonin that assists the folding
of many newly synthesized proteins in Escherichia coli and the refolding in vitro, with the …

Chaperones play a vital role in the life of cells by facilitating the correct folding of other
proteins and maintaining them in a functional state, being themselves, as a rule, more stable …

Publisher Summary Chaperonins are a group of molecular chaperones that are classified
into the GroEL/HSP60 (heat shock protein 60) family. They are widely distributed from …

The hyperthermophilic archaeon Pyrococcus furiosus (Pf) grows optimally at 100° C and
encodes single genes for the Group II chaperonin (Cpn), Pf Cpn and α-crystallin homolog …

All living organisms contain a unique class of molecular chaperones called 60 kDa heat
shock proteins (HSP60–also known as GroEL in bacteria). While some organisms contain …