Most molecular processes in living organisms rely on protein-protein interactions, many of which are mediated by β-sheet interfaces; this study investigates the formation of β-sheet interfaces through the conversion of coils into β-strands. Following an exhaustive search in the Protein Data Bank, the corresponding structural dimorphic fragments were extracted, characterized, and analyzed. Their short strand lengths and specific amino acid profiles indicate that dimorphic β-strand interfaces are likely to be less stable than standard ones and could even convert to coil interfaces if their environment changes. Moreover, the construction of a simple classifier able to discriminate between the sequences of dimorphic and standard β-strand interfaces suggests that the nature of those dimorphic sequences could be predicted, providing a novel means of identifying proteins capable of forming dimers.
Keywords: dimorphic sequences; intermolecular β-strand interfaces; protein conformational change; protein dimerization; protein structure; protein-protein interaction.
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