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• W2005717963 abstract "The folding of Escherichia coli dihydrofolate reductase was examined at pH 7.8 and 15 degrees C by using stopped-flow fluorescence and absorbance spectroscopies. The formation of a highly fluorescent intermediate occurs with relaxation times ranging between 142 and 343 msec, whereas stopped-flow absorbance spectroscopy using methotrexate binding assays shows a distinct lag phase during these time frames for the native state. The lag in absorbance kinetics and the lack of fast-track folding events indicate that the formation of this ensemble of intermediates is an obligatory step in the folding reaction." @default.
• W2005717963 created "2016-06-24" @default.
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• W2005717963 date "2000-05-16" @default.
• W2005717963 modified "2023-09-27" @default.
• W2005717963 title "An essential intermediate in the folding of dihydrofolate reductase" @default.
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• W2005717963 doi "https://doi.org/10.1073/pnas.100547697" @default.
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