New charge-bearing amino acid residues that promote β-sheet secondary structure.

ABSTRACT: 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 virtue of β-branching, and also bear an ionizable group in the side chain.

SUBMITTER: Maynard SJ 

PROVIDER: S-EPMC4277779 | biostudies-literature | 2014 Nov

REPOSITORIES: biostudies-literature