The helical s constant for alanine in water derived from template-nucleated helices
- 1 August 1991
- journal article
- letter
- Published by Springer Nature in Nature
- Vol. 352 (6334) , 451-454
- https://doi.org/10.1038/352451a0
Abstract
FORMATION of α 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: σ which reflects helix initiation and s which reflects propagation of a pre-existing helix and measures helical bias1,2. Scheraga has reported s values for oligopeptides of about 1.1, implying a weak helical bias for amino-acid residues3. By contrast, certain helical peptides studied by Baldwin seem to require much larger s values for alanine4. 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.Keywords
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