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- W2026255265 abstract "The 15N-labeled C-terminal functional domain of the bacteriophage P22 scaffolding protein was expressed and purified. The NMR chemical-shift assignments of this functional domain were determined. An analysis of the chemical shift indices for the α-protons indicates that the N-terminal half of this protein is unstructured whereas the C-terminal half is defined by a helix–loop–helix motif. Copyright © 1999 John Wiley & Sons, Ltd." @default.
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- W2026255265 date "1999-08-01" @default.
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- W2026255265 title "1H and15N chemical shift assignments of a carboxy-terminal functional domain of the bacteriophage P22 scaffolding protein" @default.
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- W2026255265 doi "https://doi.org/10.1002/(sici)1097-458x(199908)37:8<602::aid-mrc505>3.0.co;2-x" @default.
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