Simultaneous Measurement of Protein One-bond and Two-bond Nitrogen-carbon Coupling Constants Using an Internally Referenced Quantitative J-correlated [(15)N,(1)H]-TROSY-HNC Experiment

Overview

Journal J Biomol NMR

Publisher Springer

Specialties Molecular Biology
Nuclear Medicine

Date 2003 Mar 26

PMID 12652122

Citations 4

Authors

Hans L J Wienk

Mitcheell M Martinez

Gary N Yalloway

Jurgen M Schmidt

Carlos Perez

Heinz Ruterjans

Frank Lohr

Affiliations

Soon will be listed here.

Abstract

A quantitative J-correlation pulse sequence is described that allows simultaneous determination of one-bond and two-bond nitrogen-carbon coupling constants for protonated or deuterated proteins. Coupling constants are calculated from volume ratios between cross peaks and reference axial peaks observed in a single 3D spectrum. Accurate backbone (1)J(NC'), (1)J(NCalpha), and (2)J(NCalpha) coupling constants are obtained for the two [(15)N;(13)C]-labeled, medium-sized proteins flavodoxin and xylanase and for the [(2)H;(15)N;(13)C]-labeled, large protein DFPase. A dependence of one-bond and two-bond J(NCalpha) values on protein backbone psi torsion angles is readily apparent, in agreement with previously found correlations. In addition, the experiment is performed on isotropic as well as aligned protein to measure associated (15)N-(13)C residual dipolar couplings.

Citing Articles

Improved accuracy in measuring one-bond and two-bond (15)N, (13)C (α) coupling constants in proteins by double-inphase/antiphase (DIPAP) spectroscopy.

Lohr F, Reckel S, Stefer S, Dotsch V, Schmidt J J Biomol NMR. 2011; 50(2):167-90.

PMID: 21647741 DOI: 10.1007/s10858-011-9507-3.

Measurement of one and two bond N-C couplings in large proteins by TROSY-based J-modulation experiments.

Liu Y, Prestegard J J Magn Reson. 2009; 200(1):109-18.

PMID: 19581113 PMC: 2763284. DOI: 10.1016/j.jmr.2009.06.010.

A protein backbone psi and phi angle dependence of 2J(N(i),C alpha(i-1)): the new NMR experiment and quantum chemical calculations.

Kozminski W, Zhukov I, Pecul M, Sadlej J J Biomol NMR. 2005; 31(2):87-95.

PMID: 15772749 DOI: 10.1007/s10858-004-7563-7.

A strategy to obtain backbone resonance assignments of deuterated proteins in the presence of incomplete amide 2H/1H back-exchange.

Lohr F, Katsemi V, Hartleib J, Gunther U, Ruterjans H J Biomol NMR. 2003; 25(4):291-311.

PMID: 12766392 DOI: 10.1023/a:1023084605308.

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