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Updated: Mar 26, 2026

Protein WISDOM: A Workbench for In silico De novo Design of BioMolecules
Published on: July 25, 2013
Comparison of design strategies for α-helix backbone modification in a protein tertiary fold
Nathan A Tavenor1, Zachary E Reinert1, George A Lengyel1
1Department of Chemistry, University of Pittsburgh, Pittsburgh, PA 15260, USA. horne@pitt.edu.
Abstract:
We report here the comparison of five classes of unnatural amino acid building blocks for their ability to be accommodated into an α-helix in a protein tertiary fold context. High-resolution structural characterization and analysis of folding thermodynamics yield new insights into the relationship between backbone composition and folding energetics in α-helix mimetics and suggest refined design rules for engineering the backbones of natural sequences.
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