Cavity formation before stable hydrogen bonding in the folding of a beta-clam protein.
The time course of folding of a small beta-sheet protein reveals formation of a central ligand binding cavity before the consolidation of the native hydrogen bonding network. These results suggest that side chain interactions and not stable hydrogen bonding determine the beta-sheet architecture and play crucial roles in the overall chain topology.
Clark
P L
PL
Liu
Z P
ZP
Rizo
J
J
Gierasch
L M
LM
D006860:Hydrogen Bonding; D017510:Protein Folding; D017433:Protein Structure, Secondary; D018168:Receptors, Retinoic Acid / Q000737:chemistry*
D018168:Receptors, Retinoic Acid; C082927:retinoic acid binding protein I, cellular