Design and characterization of a homodimeric antiparallel coiled coil
Design and characterization of a homodimeric antiparallel coiled coil
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DOI：
10.1021/ja0357590
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发表时间：
2003-06-25
影响因子：
15
通讯作者：
Oakley, MG
中科院分区：
文献类型：
--
作者：
Gurnon, DG;Whitaker, JA;Oakley, MG
我们报道了第一个成功的自关联反平行线圈APH的设计。同时应用库仑组分和疏水组分导致了反平行排列的确定偏好，如高效液相色谱、沉降平衡和化学变性数据所判断的。设计的多肽具有与自然产生的亮氨酸拉链多肽相当的稳定性，并可在细菌中表达。APH的这些特性暗示了体内蛋白质融合和生物材料的潜在应用。
We report the first successful design of a self-associating antiparallel coiled coil, APH. The simultaneous application of Coulombic and hydrophobic components results in a decided preference for the antiparallel alignment as judged by HPLC, sedimentation equilibrium, and chemical denaturation data. The designed peptide is of comparable stability to naturally occurring leucine zipper peptides and can be expressed in bacteria. These properties of APH suggest potential in vivo protein fusion and biomaterials applications.