NMR resonance splitting of urea in stretched hydrogels: Proton exchange and 1H/2H isotopologues

Urea at 12 M in concentrated gelatin gel, that was stretched, gave H-1 and H-2 NMR spectral splitting patterns that varied in a predictable way with changes in the relative proportions of (H2O)-H-1 and (H2O)-H-2 in the medium. This required consideration of the combinatorics of the two amide groups in urea that have a total of four protonation/deuteration sites giving rise to 16 different isotopologues, if all the atoms were separately identifiable. The rate constant that characterized the exchange of the protons with water was estimated by back-transformation analysis of 2D-EXSY spectra. There was no H-1 NMR spectral evidence that the chiral gelatin medium had caused in-equivalence in the protons bonded to each amide nitrogen atom. The spectral splitting patterns in H-1 and H-2 NMR spectra were accounted for by intra-molecular scalar and dipolar interactions, and quadrupolar interactions with the electric field gradients of the gelatin matrix, respectively. (C) 2014 Elsevier Inc. All rights reserved.