Enumerative Discovery of Noncanonical Polypeptide Secondary Structures.

ABSTRACT: Energetically favorable local interactions can overcome the entropic cost of chain ordering and cause otherwise flexible polymers to adopt regularly repeating backbone conformations. A prominent example is the α helix present in many protein structures, which is stabilized by i, i + 4 hydrogen bonds between backbone peptide units. With the increased chemical diversity offered by unnatural amino acids and backbones, it has been possible to identify regularly repeating structures not present in proteins, but to date, there has been no systematic approach for identifying new polymers likely to have such structures despite their considerable potential for molecular engineering. Here we describe a systematic approach to search through dipeptide combinations of 130 chemically diver

SUBMITTER: Moyer AP 

PROVIDER: S-EPMC11421003 | biostudies-literature | 2024 Sep

REPOSITORIES: biostudies-literature