Struthers M D, Cheng R P, Imperiali B
Division of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena 91125, USA.
Science. 1996 Jan 19;271(5247):342-5. doi: 10.1126/science.271.5247.342.
Small proteins or protein domains generally require disulfide bridges or metal sites for their stabilization. Here it is shown that the beta beta alpha architecture of zinc fingers can be reproduced in a 23-residue polypeptide in the absence of metal ions. The sequence was obtained through an iterative design process. A key feature of the final design is the incorporation of a type II' beta turn to aid in beta-hairpin formation. Nuclear magnetic resonance analysis reveals that the alpha helix and beta hairpin are held together by a defined hydrophobic core. The availability of this structural template has implications for the development of functional polypeptides.
小蛋白质或蛋白质结构域通常需要二硫键或金属位点来实现稳定。本文表明，锌指的ββα结构可以在不含金属离子的23个残基的多肽中重现。该序列是通过迭代设计过程获得的。最终设计的一个关键特征是引入了II'型β转角以帮助形成β发夹结构。核磁共振分析表明，α螺旋和β发夹通过一个明确的疏水核心结合在一起。这种结构模板的可用性对功能性多肽的开发具有重要意义。
