title: Cavity formation before stable hydrogen bonding in the folding of a beta-clam protein.
abstract: 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.
authors.forename: P L
authors.initials: PL
authors.lastname: Clark
authors.forename: Z P
authors.initials: ZP
authors.lastname: Liu
authors.forename: J
authors.initials: J
authors.lastname: Rizo
authors.forename: L M
authors.initials: LM
authors.lastname: Gierasch
mesh_terms: D006860:Hydrogen Bonding; D017510:Protein Folding; D017433:Protein Structure, Secondary; D018168:Receptors, Retinoic Acid / Q000737:chemistry*
chemical_list: D018168:Receptors, Retinoic Acid; C082927:retinoic acid binding protein I, cellular