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We model helical polypeptides in an aqueous environment by explicitly evaluating winding probabilities of biopolymers. To account for differences in reaction to the solvent of the various types of amino acids forming the chainlike biopolymer, a length-dependent drift coefficient A(s) is used. As an application, we express A(s) in terms of a Bessel function to generate a sequence of winding and non-winding segments and compare this with the α-helical segments of myoglobin.