Ontology highlight
ABSTRACT:
SUBMITTER: Maynard SJ
PROVIDER: S-EPMC4277779 | biostudies-literature | 2014 Nov
REPOSITORIES: biostudies-literature
Maynard Stacy J SJ Almeida Aaron M AM Yoshimi Yasuharu Y Gellman Samuel H SH
Journal of the American Chemical Society 20141113 47
Proteinogenic amino acid residues that promote β-sheet secondary structure are hydrophobic (e.g., Ile or Val) or only moderately polar (e.g., Thr). The design of peptides intended to display β-sheet secondary structure in water typically requires one set of residues to ensure conformational stability and an orthogonal set, with charged side chains, to ensure aqueous solubility and discourage self-association. Here we describe new amino acids that manifest substantial β-sheet propensity, by virtu ...[more]