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Cavity formation before stable hydrogen bonding in the folding of a β-clam protein

The time course of folding of a small β-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 β-sheet architecture and play crucial roles in the overall chain topology.

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Clark, P., Liu, ZP., Rizo, J. et al. Cavity formation before stable hydrogen bonding in the folding of a β-clam protein. Nat Struct Mol Biol 4, 883–886 (1997). https://doi.org/10.1038/nsb1197-883

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