Self‐Assembly and Dynamics of Polypeptides

This work highlights the results of recent efforts to understand the hierarchical self-assembly and dynamics of polypeptides with the aid of different NMR techniques, X-ray scattering, and dielectric spectroscopy. The concerted application of these techniques sheds light on the origin of the glass transition, the persistence of the α-helical peptide secondary motif, and the effects of topology and packing on the type and persistence of secondary structures. With respect to the freezing of the dynamics at the liquid-to-glass temperature it was found that the origin of this effect is a network of defected hydrogen bonds. The presence of defected hydrogen-bonded regions reduces the persistence length of α-helices. Block copolypeptides provide means to manipulate both the type and persistence of peptide secondary structures.