title: Comparison of design strategies for α-helix backbone modification in a protein tertiary fold.
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.
authors: Department of Chemistry, University of Pittsburgh, Pittsburgh, PA 15260, USA. horne@pitt.edu.
authors: Nathan A
authors: NA
authors: Tavenor
authors: Department of Chemistry, University of Pittsburgh, Pittsburgh, PA 15260, USA. horne@pitt.edu.
authors: Zachary E
authors: ZE
authors: Reinert
authors: Department of Chemistry, University of Pittsburgh, Pittsburgh, PA 15260, USA. horne@pitt.edu.
authors: George A
authors: GA
authors: Lengyel
authors: Department of Chemistry, University of Pittsburgh, Pittsburgh, PA 15260, USA. horne@pitt.edu.
authors: Brian D
authors: BD
authors: Griffith
authors: Department of Chemistry, University of Pittsburgh, Pittsburgh, PA 15260, USA. horne@pitt.edu.
authors: W Seth
authors: WS
authors: Horne
mesh_terms: D000595:Amino Acid Sequence; D008969:Molecular Sequence Data; D017510:Protein Folding; D017434:Protein Structure, Tertiary; D011506:Proteins / Q000737:chemistry*; D017386:Sequence Homology, Amino Acid; D013816:Thermodynamics
chemical_list: D011506:Proteins