Repeat proteins are an attractive target for protein engineering and design. We have focused our attention on the design and engineering of one particular class - tetratricopeptide repeat (TPR) proteins. In previous work we have shown that the structure and stability of TPR proteins can be manipulated in a rational fashion [Cortajarena 2011; Main 2003]. Building on those studies, we have designed and characterized a number of different peptide-binding TPR modules and we have also assembled these modules into supramolecular arrays [Cortajarena 2009; Cortajarena 2008; Jackrel 2009; Kajander 2007]. Here we focus on the development of one such TPR-peptide interaction for a practical application – affinity purification. We illustrate the general utility of our designed protein interaction. Furthermore, this example highlights how basic research on protein-peptide interactions can lead to the development of novel reagents with important practical applications.
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机译：重复蛋白是蛋白质工程和设计的一个有吸引力的目标。我们将注意力集中在一种特殊类别的四三肽重复序列（TPR）蛋白的设计和工程上。在以前的工作中，我们表明可以以合理的方式操纵TPR蛋白的结构和稳定性[Cortajarena 2011; Main 2003]。在这些研究的基础上，我们设计并表征了许多不同的与肽结合的TPR模块，并且还将这些模块组装为超分子阵列[Cortajarena 2009; Cortajarena 2008；杰克雷尔2009; Kajander 2007]。在这里，我们专注于为实际应用开发一种此类TPR-肽相互作用-亲和纯化。我们说明了我们设计的蛋白质相互作用的一般用途。此外，该实例突出了对蛋白质-肽相互作用的基础研究如何导致具有重要实际应用的新型试剂的开发。
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