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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >De novo design and characterization of an apolar heliclal hairpin peptide at atomic resolution: Compaction mediated by weak interactions
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De novo design and characterization of an apolar heliclal hairpin peptide at atomic resolution: Compaction mediated by weak interactions

机译：从头设计和非极性螺旋发夹肽的原子分辨率表征：弱相互作用介导的紧实

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摘要

Design of helical super secondary structura1 motifs is expected to provide important scaffolds to incorporate functional sites, thus allowing the engineering of novel miniproteins with function. An α,β-dehydrophenylalanine containing 21-residue apo1ar peptide was designed to mimic the helical hairpin motif by using a simple geometrical design strategy. The synthetic peptide folds into the desired structure as assessed crystallographically at 1.0-A resolu- tion. The two helices of the helical-hairpin motif. connected by a flexible (GIy)4 linker. are docked to each other by the concerted influence of weak interactions. The folding of the peptide without binary patterning of amino acids, disulfide bonds. or metal ions is a remarkable observation. The results demonstrate that preferred interactions among the hydrophobic residues selectively discrimi- nate their putative partners in space, leading to the unique folding of the peptide. also a hallmark of the unique folding of hydropho- bic core in globular proteins. We demonstrate here the engineering of molecules by using weak interactions pointing to their possible further exploitation in the de novo design of protein super sec- ondary structural elements.
机译：螺旋超二级structura1基序的设计有望提供重要的支架，以整合功能位点，从而使具有功能的新型微蛋白得以工程化。通过使用简单的几何设计策略，设计了一个包含21个残基的载脂蛋白α-β-脱氢苯丙氨酸，以模拟螺旋发夹基序。如在1.0A分辨率下进行结晶学评估，合成肽可折叠成所需结构。螺旋形发夹图案的两个螺旋。通过灵活的（Gly）4链接器连接。在弱互动的共同影响下彼此对接。肽的折叠没有氨基酸，二硫键的二元模式。或金属离子是一个了不起的发现。结果表明，疏水残基之间的优选相互作用选择性地区分了其在空间中的假定配偶体，从而导致了肽的独特折叠。这也是疏水蛋白核心在球状蛋白中独特折叠的标志。我们在这里通过使用弱相互作用说明分子的工程设计，指出它们在蛋白质超二级结构元件的从头设计中可能的进一步利用。

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