Folding units in globular proteins.

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Abstract
A method to identify all compact, contiguous-chain, structural units in a globular protein from .times.-ray coordinates is presented. These units are then used to describe a complete set of hierarchic folding pathways for the molecule. The analysis shows that the larger units are combinations of smaller units, giving rise to a structural hierarchy ranging from the whole protein monomer through supersecondary structures down to individual helices and strands. There is > 1 way to assemble the protein by self-association of its compact units. However, the number of possible pathways is small.sbd.small enough to be exhaustively explored by a computer program. The hierarchic organization of compact units in protein molecules is consistent with a model for folding by hierarchic condensation. In this model, neighboring hydrophobic chain sites interact to form folding clusters, with further stepwise cluster association giving rise to a population of folding intermediates.

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