Abstract
Libraries of de novo proteins provide an opportunity to explore the structural potential of biological macromolecules that have not been biased by billions of years of evolutionary selection. Characterization of individual members of such libraries provides insight into the diversity of structure and dynamics accessible to nascent protein superfamilies in the absence of evolutionary optimization. Here we report the backbone and side chain chemical shifts of protein S836 from a superfamily of designed 4-helix bundles.
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Go, A., Kim, S., Hecht, M. et al. NMR assignment of S836: a de novo protein from a designed superfamily. Biomol NMR Assign 1, 213–215 (2007). https://doi.org/10.1007/s12104-007-9059-3
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DOI: https://doi.org/10.1007/s12104-007-9059-3