Band-selective radiofrequency pulses

Geen, Helen; Freeman, Ray

doi:10.1016/0022-2364(91)90034-q

Cited by 624 publications

(703 citation statements)

References 18 publications

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“…Narrow filled (open) rectangles denote hard 908 (1808)p ulses;the shaped symbols on the 13 Cc hannelrepresent REBURP [25] (denoted "a"), ISNOB2 [26] ("b"), EBURP2 [25] ("c") and time-reversed EBURP2 ("d") shapes, with band widths of 70 ppm for pulses applied to CO (centered at 175 ppm), and 32 ppm for pulses applied to Ca (centered at 54 ppm). Cross-polarization steps are denoted by opensymbols with alinear ramp on one of the channels.…”

Section: Application Of the Approach To The 14-merclpp Assemblymentioning

confidence: 99%

Solid‐State NMR H–N–(C)–H and H–N–C–C 3D/4D Correlation Experiments for Resonance Assignment of Large Proteins

et al. 2017

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Solid‐state NMR spectroscopy can provide insight into protein structure and dynamics at the atomic level without inherent protein size limitations. However, a major hurdle to studying large proteins by solid‐state NMR spectroscopy is related to spectral complexity and resonance overlap, which increase with molecular weight and severely hamper the assignment process. Here the use of two sets of experiments is shown to expand the tool kit of 1H‐detected assignment approaches, which correlate a given amide pair either to the two adjacent CO–CA pairs (4D hCOCANH/hCOCAcoNH), or to the amide 1H of the neighboring residue (3D HcocaNH/HcacoNH, which can be extended to 5D). The experiments are based on efficient coherence transfers between backbone atoms using INEPT transfers between carbons and cross‐polarization for heteronuclear transfers. The utility of these experiments is exemplified with application to assemblies of deuterated, fully amide‐protonated proteins from approximately 20 to 60 kDa monomer, at magic‐angle spinning (MAS) frequencies from approximately 40 to 55 kHz. These experiments will also be applicable to protonated proteins at higher MAS frequencies. The resonance assignment of a domain within the 50.4 kDa bacteriophage T5 tube protein pb6 is reported, and this is compared to NMR assignments of the isolated domain in solution. This comparison reveals contacts of this domain to the core of the polymeric tail tube assembly.

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Section: Application Of the Approach To The 14-merclpp Assemblymentioning

confidence: 99%

Solid‐State NMR H–N–(C)–H and H–N–C–C 3D/4D Correlation Experiments for Resonance Assignment of Large Proteins

et al. 2017

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“…Selective inversion of the water resonance was achieved by application of 2 ms shaped pulses with RE-BURP (Geen and Freeman 1991) profile. 15 N decoupling during acquisition was achieved using GARP-sequence.…”

Section: Nmr Spectroscopymentioning

confidence: 99%

19F-labeling of the adenine H2-site to study large RNAs by NMR spectroscopy

et al. 2015

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In comparison to proteins and protein complexes, the size of RNA amenable to NMR studies is limited despite the development of new isotopic labeling strategies including deuteration and ligation of differentially labeled RNAs. Due to the restricted chemical shift dispersion in only four different nucleotides spectral resolution remains limited in larger RNAs. Labeling RNAs with the NMR-active nucleus 19

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“…The shaped pulse, labeled a, is of the 180 • selective inversion IBURP2 type (Geen and Freeman, 1991), and is applied to C 6 to remove any dephasing resulting from 1 J C5C6 . The subsequent refocusing REBURP pulse, marked b, and delay τ compensate for C 5 chemical shift evolution that occurred during pulse a, and allow time for pulsed field gradient phase-encoding, enabling gradient-enhanced magnetization transfer from C 5 (at time ii) to H 5 (at time iii).…”

Section: Measurement Of Couplings In Pyrimidinesmentioning

confidence: 99%

Resolution-optimized NMR measurement of 1DCH, 1DCC and 2DCH residual dipolar couplings in nucleic acid bases

et al. 2004

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New methods are described for accurate measurement of multiple residual dipolar couplings in nucleic acid bases. The methods use TROSY-type pulse sequences for optimizing resolution and sensitivity, and rely on the E.COSY principle to measure the relatively small two-bond 2 D CH couplings at high precision. Measurements are demonstrated for a 24-nt stem-loop RNA sequence, uniformly enriched in 13 C, and aligned in Pf1. The recently described pseudo-3D method is used to provide homonuclear 1 H-1 H decoupling, which minimizes cross-correlation effects and optimizes resolution. Up to seven 1 H-13 C and 13 C-13 C couplings are measured for pyrimidines (U and C), including 1 ). Only three dipolar couplings are linearly independent in planar structures such as nucleic acid bases, permitting cross validation of the data and evaluation of their accuracies. For the vast majority of dipolar couplings, the error is found to be less than ±3% of their possible range, indicating that the measurement accuracy is not limiting when using these couplings as restraints in structure calculations. Reported isotropic values of the one-and two-bond J couplings cluster very tightly for each type of nucleotide.

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Band-selective radiofrequency pulses

Cited by 624 publications

References 18 publications

Solid‐State NMR H–N–(C)–H and H–N–C–C 3D/4D Correlation Experiments for Resonance Assignment of Large Proteins

Solid‐State NMR H–N–(C)–H and H–N–C–C 3D/4D Correlation Experiments for Resonance Assignment of Large Proteins

19F-labeling of the adenine H2-site to study large RNAs by NMR spectroscopy

Resolution-optimized NMR measurement of 1DCH, 1DCC and 2DCH residual dipolar couplings in nucleic acid bases

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