Department of Chemistry, University of Wisconsin, Madison, Wisconsin 53706, USA.
J Am Chem Soc. 2010 Jun 16;132(23):7868-9. doi: 10.1021/ja103233a.
We report the first high-resolution structural data for the beta/gamma-peptide 13-helix (i,i+3 C=O...H-N H-bonds), a secondary structure that is formed by oligomers with a 1:1 alternation of beta- and gamma-amino acid residues. Our characterization includes both crystallographic and 2D NMR data. Previous studies suggested that beta/gamma-peptides constructed from conformationally flexible residues adopt a different helical secondary structure in solution. Our design features preorganized beta- and gamma-residues, which strongly promote 13-helical folding by the 1:1 beta/gamma backbone.
我们报告了第一个β/γ-肽 13-螺旋(i,i+3 C=O...H-N H 键)的高分辨率结构数据,这是一种由β-和γ-氨基酸残基 1:1 交替组成的寡聚物形成的二级结构。我们的表征包括晶体学和 2D NMR 数据。先前的研究表明,由构象灵活的残基构成的β/γ-肽在溶液中采用不同的螺旋二级结构。我们的设计特点是预组织的β-和γ-残基,它们通过 1:1 的β/γ 主链强烈促进 13-螺旋折叠。