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• W2005208986 abstract "Eosin–5-maleimide (EM) is an increasingly important and widely used probe in the study of membrane protein structure and function. Yet little is known about its spectral properties in hydrophobic and hydrophilic environments. Furthermore, EM is hydrolyzed faster than the traditionalN-ethylmaleimide. To offer a more solid foundation for the use of EM in studies of membrane protein structure and function, we have undertaken a detailed study of the absorbance and fluorescence spectra of EM, eosin–5-maleic acid, and thel-cysteine and β-mercaptoethanol adducts of EM in aqueous and hydrophobic environments; we have studied the kinetics of hydrolysis of EM in various environments, and we have investigated the reaction kinetics of EM withl-cysteine." @default.
• W2005208986 created "2016-06-24" @default.
• W2005208986 creator A5059293761 @default.
• W2005208986 creator A5085576102 @default.
• W2005208986 date "1998-03-01" @default.
• W2005208986 modified "2023-10-18" @default.
• W2005208986 title "Spectroscopic and Kinetic Characterization of Eosin–5-Maleimide" @default.
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• W2005208986 doi "https://doi.org/10.1006/abio.1998.2575" @default.
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