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Physicochemical Characteristics of a Variant of Chaperon GroEL Apical Domain Designed to Enhance the Expression and Stability of Target Proteins
Applied Biochemistry and Microbiology ( IF 1.0 ) Pub Date : 2019-12-05 , DOI: 10.1134/s0003683819080088 K. A. Kurov , O. I. Savvin , M. S. Yurkova , V. A. Zenin , G. S. Nagibina , B. S. Melnik , A. N. Fedorov
中文翻译:
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
更新日期:2019-12-05
Applied Biochemistry and Microbiology ( IF 1.0 ) Pub Date : 2019-12-05 , DOI: 10.1134/s0003683819080088 K. A. Kurov , O. I. Savvin , M. S. Yurkova , V. A. Zenin , G. S. Nagibina , B. S. Melnik , A. N. Fedorov
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:
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