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- W2008904725 abstract "We recently found that the larger parts of the endocytic proteins epsin 1 and AP180 consist of an unstructured polypeptide chain. As a result these segments are completely heat-stable without loss of their functional properties. We have taken advantage of this fact and developed a combined heat lysis and pre-purification procedure after expressing the disordered domains in E. coli. This results in the irreversible denaturation and precipitation of the majority of bacterial proteins. The bacteria are resuspended in a non-denaturing buffer, heated in a boiling water bath and shock-cooled. We demonstrate that this procedure compared to conventional lysis improves both yield and quality of the purified protein." @default.
- W2008904725 created "2016-06-24" @default.
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- W2008904725 date "2003-03-25" @default.
- W2008904725 modified "2023-09-27" @default.
- W2008904725 title "A novel strategy for the purification of recombinantly expressed unstructured protein domains" @default.
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- W2008904725 doi "https://doi.org/10.1016/s1570-0232(02)00908-x" @default.
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