Novel protein structural motifs containing two-turn and longer 3(10)-helices.

The 3(10)-helix constitutes a small but significant fraction of secondary structural elements in proteins. Protein data base surveys have shown these helices to be present as alpha-helical extensions, in loops and as connectors between beta-strands. The present work focuses on two-turn and longer 3(10)-helices where we establish that two-turn and longer 3(10) helices, unlike the more abundant single-turn 3(10)-helices, frequently occur independent of any other contiguous secondary structural elements. More importantly, a large fraction of these independent two-turn and longer 3(10)-helices, along with alpha-helices and beta-strands, are found to form novel super-secondary structural motifs in several proteins with possible implications for protein folding, local conformational relaxation and biological functions.