|New Crystal Structures Lift Fog around Protein Folding|
Nature's proteins set a high bar for nanotechnology.
Macromolecules forged from peptide chains of amino acids, these
biomolecular nanomachines must first be folded into a dazzling
variety of shapes and forms before they can perform the
multitude of functions fundamental to life. However, the
mechanisms behind the protein-folding process have remained a
foggy mystery. Now the fog is lifting: a team of researchers
from Berkeley Lab, Stanford University, and the Massachusetts
Institute of Technology has deciphered the crystal structure of
a critical control element within chaperonin, the protein
complex responsible for the correct folding of other proteins.
Chaperonins promote the proper folding of newly translated
proteins and proteins that have been stress-denatured—meaning
they've lost their structure—by encapsulating them inside a
protective chamber formed from two rings of molecular complexes
stacked back-to-back. There are two classes of chaperonins,