在体检测和定量分析增强蛋白质稳定性的化学物质。
In vivo detection and quantification of chemicals that enhance protein stability.
机构信息
Howard Hughes Medical Institute, Department of Molecular, Cellular, and Developmental Biology, University of Michigan, Ann Arbor, MI 48109, USA.
出版信息
Anal Biochem. 2013 Mar 1;434(1):181-6. doi: 10.1016/j.ab.2012.11.022. Epub 2012 Dec 5.
Abstract
We have devised protein-folding sensors that link protein stability to TEM-1 β-lactamase activity. The addition of osmolytes and other compounds with chemical chaperone activity to the growth medium of bacteria containing these sensors increases β-lactamase activity up to 207-fold in a dose-dependent manner. This enables the rapid detection and sensitive quantification of compounds that enhance in vivo protein stability.
摘要
我们设计了一种蛋白质折叠传感器，将蛋白质稳定性与 TEM-1 β-内酰胺酶活性联系起来。在含有这些传感器的细菌生长培养基中添加渗透剂和其他具有化学伴侣活性的化合物，可使β-内酰胺酶活性在剂量依赖性的方式下增加 207 倍。这使得能够快速检测和灵敏地定量增强体内蛋白质稳定性的化合物。
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