schematikon: Detailed Sequence-Structure Relationships from Mining a Non-redundant Protein Structure Database

If a "protein folding code" exists, it ought to give rise to detectable sequence propensities that are associated with low energy conformations, i.e. native structure. To the degree that the frequency of structure patterns in folded proteins has a Boltzmann-like behaviour, such conformations should be detectable by their excess occurrence over random. We have mined a database of non-homologous, well resolved protein structure domains – Nh3D – and have discovered an abundance of such sets of overrepresented structurally similar patterns. We designate the best representatives of a set a motif. Our motif dictionary schematikon shows significant and interesting sequence propensities and is predictive regarding the experimentally determined consequences of sequence change on stability.