Comparison of design strategies for ?-helix backbone modification in a protein tertiary fold.
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ABSTRACT:
SUBMITTER: Tavenor NA
PROVIDER: S-EPMC4767680 | biostudies-literature | 2016 Mar
REPOSITORIES: biostudies-literature
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Comparison of design strategies for α-helix backbone modification in a protein tertiary fold.
Tavenor Nathan A NA Reinert Zachary E ZE Lengyel George A GA Griffith Brian D BD Horne W Seth WS
Chemical communications (Cambridge, England) 20160301 19
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. ...[more]
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