The helical s constant for alanine in water derived from template-nucleated helices.

Abstract

Formation of alpha helices from disordered polypeptides depends on the degree to which amino acids favour the helical state. The folding of helical oligopeptides can be modelled by two parameters: sigma which reflects helix initiation and s which reflects propagation of a pre-existing helix and measures helical bias. Scheraga has reported s values for oligopeptides of about 1.1, implying a weak helical bias for amino-acid residues. By contrast, certain helical peptides studied by Baldwin seem to require much larger s values for alanine. Resolution of this inconsistency requires experiments that disentangle the ease of propagation from that of initiation. In this study varying lengths of polyalanine are linked to a 'template' that initiates helical structure and permits study solely of propagation. We report here that the s value for alanine in water is close to 1, supporting the earlier results of Scheraga but not the more recent results of Baldwin.