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• W2017235724 abstract "In proteomic research, it is often necessary to screen a large number of polypeptides for the presence of stable structure. Described here is a technique (referred to as SUPREX, stability of unpurified proteins from rates of H/D exchange) for measuring the stability of proteins in a rapid, high-throughput fashion. The method uses hydrogen exchange to estimate the stability of microgram quantities of unpurified protein extracts by using matrix-assisted laser desorption/ionization MS. The stabilities of maltose binding protein and monomeric lambda repressor variants determined by SUPREX agree well with stability data obtained from conventional CD denaturation of purified protein. The method also can detect the change in stability caused by the binding of maltose to maltose binding protein. The results demonstrate the precision of the method over a wide range of stabilities." @default.
• W2017235724 created "2016-06-24" @default.
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• W2017235724 date "2000-07-11" @default.
• W2017235724 modified "2023-10-16" @default.
• W2017235724 title "A quantitative, high-throughput screen for protein stability" @default.
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• W2017235724 doi "https://doi.org/10.1073/pnas.140111397" @default.
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