Hairpin Folding Behavior of Mixed α/β-Peptides in Aqueous Solution

被引:44
作者
Lengyel, George A. [1 ]
Frank, Rebecca C. [1 ]
Horne, W. Seth [1 ]
机构
[1] Univ Pittsburgh, Dept Chem, Pittsburgh, PA 15260 USA
关键词
SHEET SECONDARY STRUCTURE; BETA-HAIRPIN; AROMATIC INTERACTIONS; AMINO-ACIDS; FOLDAMERS; HELIX; SEQUENCE; DESIGN; MODEL; STABILITY;
D O I
10.1021/ja2002346
中图分类号
O6 [化学];
学科分类号
0703 ;
摘要
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 a-helix, mimicry of protein beta-sheets is less understood. We report here the aqueous folding behavior of a prototype alpha-peptide hairpin model sequence varied at cross-strand positions by incorporation of 16 different beta-amino acid monomers. Our results provide a folding propensity scale for beta-residues in a protein beta-sheet context as well as high-resolution structures of several mixed-backbone alpha/beta-peptide hairpins in water.
引用
收藏
页码:4246 / 4249
页数:4
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