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Default 14N NMR relaxation times of several protein amino acids in aqueous solution--comparis

14N NMR relaxation times of several protein amino acids in aqueous solution--comparison with 17O NMR data and estimation of the relative hydration numbers in the cationic and zwitterionic forms.

Related Articles 14N NMR relaxation times of several protein amino acids in aqueous solution--comparison with 17O NMR data and estimation of the relative hydration numbers in the cationic and zwitterionic forms.

J Magn Reson. 2003 Oct;164(2):294-303

Authors: Troganis AN, Tsanaktsidis C, Gerothanassis IP

The 14N nuclear magnetic resonance (NMR) linewidths of the alpha-amino groups of several protein amino acids were measured in aqueous solution, with and without composite proton decoupling, to estimate the effect of proton exchange and molecular weight on the linewidths. It is shown that, contrary to earlier claims, the increase in the linewidth at low pH is not exclusively due to the effect of proton exchange broadening. The 14N linewidths, under composite proton decoupling, increase with the bulk of the amino acid, and increase at low pH. Statistical treatment of the experimental 14N and literature 17O NMR data was performed assuming two models: (i) an isotropic molecular reorientation of a rigid sphere in a medium of viscosity eta, (ii) a stochastic diffusion of the amino and carboxyl groups comprising contributions from internal (tauint) and overall (taumol) motions. Assuming a single correlation time from overall molecular reorientation (taumol), then, a linear correlation was found between the linewidths and the molecular weights of the protein amino acids at the pH values 0.5 and 6.0, which are characteristic of the cationic and zwitterionic forms, respectively. The slopes of the straight-lines were found to be dependent of pH for 14N, contrary to the 17O linear correlations whose slopes were found to be independent of pH. Assuming effective correlation times of the amino and carboxyl groups, which comprise contributions from the internal (tauint) and overall (taumol) motions, then, a significant improvement of the statistics of the regression analysis was observed. The 14N relaxation data, in conjunction with 17O NMR linewidths, can be interpreted by assuming that the 14N quadrupole coupling constants (NQCCs) are influenced by the protonation state of the carboxyl group, the 17O NQCCs remain constant, and the cationic form of the amino acids is hydrated by an excess of 1-3 molecules of water relative to the zwitterionic state.

PMID: 14511597 [PubMed - indexed for MEDLINE]



Source: PubMed
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