Hairpin folding behavior of mixed α/β-peptides in aqueous solution
| Autor: | George A. Lengyel, W. Seth Horne, Rebecca C. Frank |
|---|---|
| Rok vydání: | 2011 |
| Předmět: |
chemistry.chemical_classification
Models Molecular Protein Folding Aqueous solution Stereochemistry A protein Water Context (language use) Sequence (biology) General Chemistry Biochemistry Catalysis Protein Structure Secondary Amino acid Folding (chemistry) Solutions chemistry.chemical_compound Crystallography Colloid and Surface Chemistry Monomer chemistry Peptides |
| Zdroj: | Journal of the American Chemical Society. 133(12) |
| ISSN: | 1520-5126 |
| Popis: | The invention of new strategies for the design of protein-mimetic oligomers that manifest the folding encoded in natural amino acid sequences is a significant challenge. In contrast to the α-helix, mimicry of protein β-sheets is less understood. We report here the aqueous folding behavior of a prototype α-peptide hairpin model sequence varied at cross-strand positions by incorporation of 16 different β-amino acid monomers. Our results provide a folding propensity scale for β-residues in a protein β-sheet context as well as high-resolution structures of several mixed-backbone α/β-peptide hairpins in water. |
| Databáze: | OpenAIRE |
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