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The N−H bond length in backbone peptide groups of the protein GB3 has been studied by liquid-crystal NMR, using five structurally conserved mutants of this protein. In the absence of additional information, the impact of dynamic fluctuations of the N−H vector orientation on the 15N−1H dipolar interaction cannot be separated from a change in N−H bond length. However, a change in N−H bond length directly impacts the orientation of C′−H vectors in the peptide group, and simultaneous analysis of 13C′−HN and 15N−HN residual dipolar couplings, measured under five different alignment orientations, permits modelfree determination of the average equilibrium N−H bond length in GB3, yielding rNHeq = 1.008 ± 0.006 A. Anharmonicity of the bond stretching results in a slightly longer time-averaged bond length = 1.015 ± 0.006 A, and an effective bond length reff = −1/3 = 1.023 ± 0.006 A pertinent for NMR relaxation analysis, not including the impact of zero-point or other angular fluctuations in N−H orienta...

NMR Determination of Amide N−H Equilibrium Bond Length from Concerted Dipolar Coupling Measurements