Variants of 310‐helices in proteins

An analysis of the shortest 310‐helices, containing three helical residues and two flanking capping residues that participate in two consecutive i + 3 → i hydrogen bonds, shows that not all helices belong to the classic 310‐helix, where the three central residues adopt the right‐handed helical conformation (αR). Three variants identified are: 3  L10 ‐helix with all residues in the left‐handed helical region (αL), 3  EL10 ‐helix where the first residue is in the extended region followed by two residues in the αL conformation, and its mirror‐image, the 3  E′R10 ‐helix. In the context of these helices, as well as the equivalent variants of α‐helices, the length dependence of the handedness of secondary structures in protein structure is discussed. There are considerable differences in the amino acid preferences at different positions in the various types of 310‐helices. Each type of 310‐helix can be thought to be made up of an extension of a particular type of β‐turn (made up of residues i to i + 3) such that the (i + 3)th residue assumes the same conformation as the preceding residue. Distinct residue preferences at i and i + 3 positions seem to decide whether a particular stretch of four residues will be a β‐turn or a 310‐helix in the folded structure. Proteins 2002;48:571–579. © 2002 Wiley‐Liss, Inc.

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