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

ABSTRACT: Proteinogenic amino acid residues that promote ?-sheet secondary structure are hydrophobic (e.g., Ile or Val) or only moderately polar (e.g., Thr). The design of peptides intended to display ?-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 ?-sheet propensity, by virtue of ?-branching, and also bear an ionizable group in the side chain.

SUBMITTER: Maynard SJ 

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

REPOSITORIES: biostudies-literature

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

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]

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