Cell Chaperones Keep Proteins Properly Folded
August 2, 2011
Imagine linking together a chain of 300 plastic shapes, some with magnets at various places. Then let it go and see if you could get it to fold spontaneously into a teapot. This is the challenge that cells face every minute: folding long chains of amino acids (polypeptides) into molecular machines and structures for the cell’s numerous tasks required for life. DNA in the nucleus codes for these polypeptides. They are assembled in ribosomes in single-file order. How do they end up in complex folded shapes? Some polypeptides will spontaneously collapse into their native folds, like the magnetic chain in our analogy. Others, however, need help. Fortunately, the cell provides an army of assistants, called chaperones, to monitor, coax, and repair unfolded proteins, to achieve “proteostasis” – a stable, working set of proteins. That army is so well-organized and complex, scientists continue to try to figure out how it performs so well in the field.
