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• W2147840867 abstract "The beta/A4-amyloid protein (beta/A4) and many synthetic fragments of this protein have proved to be very difficult to solubilize, leading to the use of relatively harsh chemical methods, most notably, formic acid. This treatment has previously been shown to cause a covalent modification of this peptide. In this study, one- and two-dimensional NMR techniques are used to show that the nature of this covalent modification is formation of a formate ester to a serine residue. This finding is consistent with our previously reported kinetic studies of formic acid-induced modification of beta/A4 and further illustrates the potential danger of solubilizing fragments of beta/A4 in formic acid. Alternative methods of solubilization are discussed." @default.
• W2147840867 created "2016-06-24" @default.
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• W2147840867 date "2008-06-28" @default.
• W2147840867 modified "2023-09-24" @default.
• W2147840867 title "NMR Identification of the Formic Acid-Modified Residue in Alzheimer's Amyloid Protein" @default.
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• W2147840867 doi "https://doi.org/10.1046/j.1471-4159.1994.62010349.x" @default.
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