A new method for the measurement of homonuclear 3 J(H N H ␣ ) coupling constants in 15 N-labeled small proteins is described. The method is based on a modified sensitivity enhanced HSQC experiment, where the 3 J(H N H ␣ ) couplings are multiplied in the f 1dimension. The J-multiplication of homonucl
A J-Multiplied HMQC (MJ-HMQC) Experiment for Measuring 3JHNHα Coupling Constants
✍ Scribed by Youlin Xia; Xiangming Kong; Nancy Ip; Guang Zhu
- Publisher
- Elsevier Science
- Year
- 2000
- Tongue
- English
- Weight
- 68 KB
- Volume
- 146
- Category
- Article
- ISSN
- 1090-7807
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✦ Synopsis
amplifies J coupling constants m times and allows direct observation of the 3 J HNH␣ coupling constants of peptides and proteins (<10 kDa). The drawbacks to this method are line broadening in the f 1 -dimension and lower sensitivity. In the J-multiplied HMQC (MJ-HMQC) experiment described here, the PEP-HSQC pulse sequence is replaced by a sensitivity-enhanced HMQC section, and the total decay time for the J-coupling and the chemical shift evolution is shortened by a period of t 1 . This experiment affords narrower linewidth and enhances the sensitivity by 34%, on an average of 105 well-isolated peaks, when compared with the MJ-HSQC experiment.
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A new HMQC-based experiment is presented which allows for an efficient determination of accurate homonuclear coupling-constant values. Pure absorption lineshapes with tilted cross-peak patterns are obtained by a combination of the active-couplingpattern tilting (ACT) scheme with J-scaling. Character
## Abstract Efficient pulse sequences for measuring ^1^H–^1^H coupling constants (__J__~HH~) in strongly coupled spin systems, named selective __J__‐resolved‐HMQC‐1 and ‐2, have been developed. In the strongly coupled spin systems such as ‐CH~2~‐CH~A~(OH)‐CH~B~(OH)‐CH~2~‐, measurements of ^3^__J__~