Abstract

This work describes the properties of a new protein, a modification of GroEL apical domain designed to be a leader in fusion systems. This polypeptide leader demonstrates a high level of expression in a bacterial system; it is soluble and retains its solubility during standard biochemical manipulations. The secondary structure of the protein and its thermostability, as well as the protein solubility, were studied in a wide temperature range. To simplify the subsequent purification of the target protein, the possibility of its chemical cleavage from the fused protein by methionine residues with cyanogen bromide is provided.

中文翻译：

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旨在增强靶蛋白表达和稳定性的伴侣GroEL顶端结构域变体的理化特性

摘要

这项工作描述了一种新蛋白的特性，该蛋白是GroEL顶端结构域的一种修饰，旨在成为融合系统的领导者。该多肽前导序列在细菌系统中显示出高水平的表达。它是可溶的，并在标准生化操作中保持其溶解性。在较宽的温度范围内研究了蛋白质的二级结构及其热稳定性以及蛋白质的溶解度。为了简化目标蛋白的后续纯化，提供了用溴化氰通过蛋氨酸残基从融合蛋白上化学裂解其可能性的方法。