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- W2006876295 abstract "The largest subunit of RNA polymerase II has an interesting C-terminal domain, which consists of a multiple tandem repeat of a heptapeptide with the consensus sequence Ser–Pro–Thr–Ser–Pro–Ser–Tyr. However, the functional role of this sequence is unclear. One might assume that the conformation of the tandem repeat is very important for its function. The conformation of poly(Ser–Pro–Thr–Ser–Pro–Ser–Tyr) and H–Ser–Pro–Thr–Ser–Pro–Ser–Tyr–OH, corresponding to the repeat and the repeating unit of the C-terminal domain, respectively, were investigated exhaustively by circular dichroism (CD). The CD spectrum of H–Ser–Pro–Thr–Ser–Pro–Ser–Tyr–OH indicated the presence of a turn structure in water, which was further stabilized in 2,2,2-trifluoroethanol (TFE) and in acetonitrile. The CD spectra of the polyheptapeptide poly(Ser–Pro–Thr–Ser–Pro–Ser–Tyr) suggested that the disordered conformation was predominant in water and that the turn structure was stabilized by increasing the content of TFE or acetonitrile in the ..." @default.
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- W2006876295 date "2001-06-01" @default.
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- W2006876295 title "Conformational Study of the Tandem Repeat Sequence in RNA Polymerase II by Circular Dichroism Spectroscopy" @default.
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- W2006876295 doi "https://doi.org/10.1246/bcsj.74.1139" @default.
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