Comparison of design strategies for α-helix backbone modification in a protein tertiary fold. Issue 19 (8th February 2016)

• Record Type: Journal Article
• Authors: Tavenor, Nathan A.; Reinert, Zachary E.; Lengyel, George A.; Griffith, Brian D.; Horne, W. Seth
• Is Part Of: Chemical communications. Volume 52:Issue 19(2016)
• Page Start: 3789
• Page End: 3792
• Publication Date: 2016-02-08
• Subjects: Chemistry -- Periodicals; 540
• DOI: 10.1039/c6cc00273k
• Languages: English
• ISSNs: 1359-7345

Abstract

Abstract : Structural and thermodynamic analysis of a family of synthetic proteins with heterogeneous backbones yields new insights into the ability of unnatural amino acids to be accommodated into α-helices. 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.