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Dynamics of Random Hydrophobic-Hydrophilic Copolymers with Implications for Protein Folding.

We study the dynamics of a single amphiphilic random copolymer chain. The dynamical treatment shows that in addition to the collapse temperature, T θ , there exists a scale dependent glass transition temperature T G (l). Distinct scenarios for the glassy behavior emerges depending on the relative values of T θ and T G (l). The possible implications of our results for protein folding, including an estimate of the dependence of the ratio of the folding transition temperature to T G (l) on the length of the chain, are sketched.