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Helix-loop-helix peptide foldamers and their use in the construction of hydrolase mimetics.

08:00 EDT 17th July 2018 | BioPortfolio

Summary of "Helix-loop-helix peptide foldamers and their use in the construction of hydrolase mimetics."

De novo designed helix-loop-helix peptide foldamers containing cis-2-aminocyclopentanecarboxylic acid residues were evaluated for their conformational stability and possible use in enzyme mimetic development. The correlation between hydrogen bond network size and conformational stability was demonstrated through CD and NMR spectroscopies. Molecules incorporating a Cys/His/Glu triad exhibited enzyme-like hydrolytic activity.

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This article was published in the following journal.

Name: Bioorganic chemistry
ISSN: 1090-2120
Pages: 356-361

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Medical and Biotech [MESH] Definitions

A subfamily of HELIX-TURN-HELIX DNA-binding proteins that contain a variable length loop adjacent to the HTH motif. The loop connects two anti-parallel strands and forms a wing when bound to DNA.

A family of DNA-binding transcription factors that contain a basic HELIX-LOOP-HELIX MOTIF.

A family of transcription factors that contain regions rich in basic residues, LEUCINE ZIPPER domains, and HELIX-LOOP-HELIX MOTIFS.

Recurring supersecondary structures characterized by 20 amino acids folding into two alpha helices connected by a non-helical "loop" segment. They are found in many sequence-specific DNA-BINDING PROTEINS and in CALCIUM-BINDING PROTEINS.

A negative regulator of BASIC HELIX-LOOP-HELIX TRANSCRIPTION FACTORS. It plays a role in regulating IMMUNOGLOBULIN E expression.

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