Hannah K. Murnen

TL;DR: The aqueous self-assembly of a sequence-specific bioinspired peptoid diblock copolymer into monodisperse superhelices is demonstrated to be the result of a hierarchical process, strongly dependent on the charging level of the molecule.

TL;DR: In this paper, a series of peptoid homopolymers are stable up to temperatures of 250−300 °C and are crystalline with reversible melting transitions ranging from 150 to 225 °C.

TL;DR: Polypeptoids, which lack backbone hydrogen bonding and chirality, are used to probe the exclusive effect of hydrophobicity on the coil-to-globule collapse and two sequences containing the same composition of only hydrophobic “H’ N-methylglycine and polar “P” N-(2-carboxyethyl)glycines are shown to have very different globule collapse behaviors.

TL;DR: In this article, the relationship between main chain helicity in polypeptoid chains and persistence length is investigated, and it is shown that polypeptic chains with aromatic phenyl side chains are inherently flexible with persistence lengths ranging from 0.5 to 1 nm.

TL;DR: In this paper, a biomimetic poly N-substituted glycines (polypeptoids) have been designed to position charged side chains at precise distances from each other to elucidate the relationship between the spacing of the charges along the backbone, the ionic strength, and the persistence length.