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This work is a first attempt to characterise the conformational preference of structurally ambivalent helices in terms of their backbone conformational entropy. Ambivalent sequences conform to two different secondary structures (helix-sheet or helix-random coil or sheet-random coil, etc.) in two different proteins. For variable ambivalent helices, the helical conformations are found to possess less conformational entropy as compared with their non-helical counterparts when the ϕ-ψ dihedral angle range of the entire peptide segment is used to calculate the backbone conformational entropy. The favourable number of native contacts is a primary stabilising factor for these helical conformations. However, an opposite trend is observed when the ϕ-ψ angles of the individual amino acids are used to calculate the backbone conformational entropy. The results show that these peptide segments are rather reluctant to form helices, but are driven to form helices due to the favourable number of native contacts and optimum range of ϕ-ψ angle of the segments. Both procedures are validated by applying on conserved helices in the non-redundant database and their corresponding counterparts in the Structural Classification of Proteins database. Although context is a major determinant in deciding conformations of ambivalent sequences, no significant difference in the conformational entropy of sequences flanking ambivalent helical sequences in helical and non-helical forms is observed in this study. The results may be useful in understanding the structural context and environmental factors which leads to the formation of ambivalent helices and designing de novo proteins.

Are ambivalent α-helices entropically driven?