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• W2157234080 abstract "Analogous to the recently introduced ARTSY method for measurement of one-bond 1H–15N residual dipolar couplings (RDCs) in large perdeuterated proteins, we introduce methods for measurement of base 13C–1H and 15N–1H RDCs in protonated nucleic acids. Measurements are based on quantitative analysis of intensities in 1H–15N and 13C–1H TROSY-HSQC spectra, and are illustrated for a 71-nucleotide adenine riboswitch. Results compare favorably with those of conventional frequency-based measurements in terms of completeness and convenience of use. The ARTSY method derives the size of the coupling from the ratio of intensities observed in two TROSY-HSQC spectra recorded with different dephasing delays, thereby minimizing potential resonance overlap problems. Precision of the RDC measurements is limited by the signal-to-noise ratio, S/N, achievable in the 2D TROSY-HSQC reference spectrum, and is approximately given by 30/(S/N) Hz for 15N–1H and 65/(S/N) Hz for 13C–1H. The signal-to-noise ratio of both 1H–15N and 1H–13C spectra greatly benefits when water magnetization during the experiments is not perturbed, such that rapid magnetization transfer from bulk water to the nucleic acid, mediated by rapid amino and hydroxyl hydrogen exchange coupled with 1H–1H NOE transfer, allows for fast repetition of the experiment. RDCs in the mutated helix 1 of the riboswitch are compatible with nucleotide-specifically modeled, idealized A-form geometry and a static orientation relative to the helix 2/3 pair, which differs by ca 6° relative to the X-ray structure of the native riboswitch." @default.
• W2157234080 created "2016-06-24" @default.
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• W2157234080 date "2011-09-01" @default.
• W2157234080 modified "2023-10-17" @default.
• W2157234080 title "Measurement of 1H–15N and 1H–13C residual dipolar couplings in nucleic acids from TROSY intensities" @default.
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• W2157234080 doi "https://doi.org/10.1007/s10858-011-9544-y" @default.
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