Protein folding: the stepwise assembly of foldon units

H Maity, M Maity, MMG Krishna… - Proceedings of the …, 2005 - National Acad Sciences
H Maity, M Maity, MMG Krishna, L Mayne, SW Englander
Proceedings of the National Academy of Sciences, 2005National Acad Sciences
Equilibrium and kinetic hydrogen exchange experiments show that cytochrome c is
composed of five foldon units that continually unfold and refold even under native
conditions. Folding proceeds by the stepwise assembly of the foldon units rather than one
amino acid at a time. The folding pathway is determined by a sequential stabilization
process; previously formed foldons guide and stabilize subsequent foldons to progressively
build the native protein. Four other proteins have been found to show similar behavior …
Equilibrium and kinetic hydrogen exchange experiments show that cytochrome c is composed of five foldon units that continually unfold and refold even under native conditions. Folding proceeds by the stepwise assembly of the foldon units rather than one amino acid at a time. The folding pathway is determined by a sequential stabilization process; previously formed foldons guide and stabilize subsequent foldons to progressively build the native protein. Four other proteins have been found to show similar behavior. These results support stepwise protein folding pathways through discrete intermediates.
National Acad Sciences