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Rapid measurement of scalar three-bond 1HN-1H alpha spin coupling constants in 15N-labelled proteins.

作者信息

Ponstingl H, Otting G

机构信息

Department of Medical Biochemistry and Biophysics, Karolinska Institute, Stockholm, Sweden.

出版信息

J Biomol NMR. 1998 Aug;12(2):319-24. doi: 10.1023/a:1008293016073.

DOI:10.1023/a:1008293016073
PMID:9752002
Abstract

Two new 2D NMR experiments, CT-HMQC-HA and CT-HMQC-HN, are proposed for the rapid measurement of homonuclear 3JHNH alpha coupling constants of uniformly 15N-enriched proteins in solution. The experiments are based on the comparison of the signal intensities in a pair of constant-time [15N,1H]-HMQC spectra recorded with and without decoupling of the amide proton-alpha proton coupling. Experimental data recorded with the 78-residue N-terminal domain of the E. coli arginine repressor (ArgR-N) and with oxidized E. coli flavodoxin (176 residues) showed good agreement with 3JHNH alpha coupling constants obtained by fitting of the multiplet fine structure of the amide proton resonances or from a 3D HNHA-J experiment, respectively. Quantitative estimates for the effects from different relaxation rates of in-phase and antiphase magnetization are given.

摘要

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Protein Sci. 1997 Dec;6(12):2525-37. doi: 10.1002/pro.5560061205.
3
Solution structure of the DNA-binding domain and model for the complex of multifunctional hexameric arginine repressor with DNA.
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