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Protein Engineering, Vol. 12, No. 10, 811-814, October 1999
© 1999 Oxford University Press

Short Communications

Novel protein structural motifs containing two-turn and longer 310-helices

Lipika Pal and Gautam Basu1

Department of Biophysics, Bose Institute, P-1/12 CIT Scheme VIIM, Calcutta 700 054, India

The 310-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 ß-strands. The present work focuses on two-turn and longer 310-helices where we establish that two-turn and longer 310 helices, unlike the more abundant single-turn 310-helices, frequently occur independent of any other contiguous secondary structural elements. More importantly, a large fraction of these independent two-turn and longer 310-helices, along with {alpha}-helices and ß-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.

Keywords: 310-helix/{alpha}-helix/secondary structure/structural motif

1 To whom correspondence should be addressed; email: gautam{at}boseinst.ernet.in


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