Abstract
AbstractConditions for the occurrence of one, two, and even three helix–coil transitions are summarized and further delineated in terms of thermodynamic parameters in simple modifications of a 2 × 2 matrix of statistical weights for amino acid residues in the coiled and helical conformations. Solvent interaction with segments in both the exposed, coiled and compact, helical conformations is worked into the model. Theoretical expressions for the temperature dependence of helical fractions, maximum attained degrees of helicity, and the compositional dependence of transition temperatures are compared with experimental data for two synthetic polypeptides that exhibit multiple helix–coil transitions.
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