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- W2051139617 abstract "Two models of the repeating C-terminal domain of RNA polymerase II (Ac−SYSPTSPSYS−NH2; Ac−SYSPT(β-O-GlcNAc)SPSYS−NH2) were prepared and their conformations in water studied using 1-D and 2-D 1H NMR spectroscopies, CD spectrophotometry, fluorescence anisotropy, and molecular mechanics and dynamics calculations. The data suggest that glycosylation of the native, randomly coiled peptide with a single, biologically relevant sugar leads to the formation of a turn. This report represents the first structural study of a new class of glycoproteins monoglycosylated with N-acetylglucosamine on threonine." @default.
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- W2051139617 date "1998-11-01" @default.
- W2051139617 modified "2023-10-16" @default.
- W2051139617 title "Glycosylation of Threonine of the Repeating Unit of RNA Polymerase II with β-Linked <i>N</i>-Acetylglucosame Leads to a Turnlike Structure" @default.
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- W2051139617 doi "https://doi.org/10.1021/ja982312w" @default.
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