Abstract
Statistical analysis of amino acid patterns in approximately 160,000 α-helices in experimentally determined structures revealed di-, tri-, and tetrapeptides, whose frequencies deviate most from the statistical model. Importantly, some sequences were never found in α- helices. This fact was detected initially with tripeptides, where nearly 1% of the possible sequences were never seen in the helical segments. For tetrapeptides, this effect is very strong and significant; almost 43% of the possible sequences never appear in α-helices. It is possible that there are some steric and energetic restrictions that do not allow these tetrameric amino acid sequences to form α-helical structure.
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