How do chaperonins fold protein?

How do chaperonins fold protein?

Protein folding is a biological process that is essential for the proper functioning of proteins in all living organisms. In cells, many proteins require the assistance of molecular chaperones for their folding. Chaperonins belong to a class of molecular chaperones that have been extensively studied. However, the mechanism by which a chaperonin mediates the folding of proteins is still controve...

How do small single-domain proteins fold?

Many small, monomeric proteins fold with simple two-state kinetics and show wide variation in folding rates, from microseconds to seconds. Thus, stable intermediates are not a prerequisite for the fast, efficient folding of proteins and may in fact be kinetic traps and slow the folding process. Using recent studies, can we begin to search for trends which may lead to a better understanding of t...

Chaperonins as protein-folding machines

The Escherichia coli chaperone GroEL epitomizes the group of chaperone proteins termed as chaperonins. The wealth of structural and functional information available for GroEL, and its accessory protein, the co-chaperonin GroES, has been of much value in deciphering the role of chaperonins in facilitating the folding of substrate proteins in the cell. The chaperonin machinery has a complex archi...

How does a simplified-sequence protein fold?

To investigate a putatively primordial protein we have simplified the sequence of a 56-residue alpha/beta fold (the immunoglobulin-binding domain of protein G) by replacing it with polyalanine, polythreonine, and diglycine segments at regions of the sequence that in the folded structure are alpha-helical, beta-strand, and turns, respectively. Remarkably, multiple folding and unfolding events ar...

How does a simplified-sequence protein fold? SUPPLEMENTARY MATERIAL