Determination of dynamic parameters in amino acids from 17O NMR line width measurements (original) (raw)

Magnetic Resonance in Chemistry, 1991

Abstract

The viscosity and temperature dependence of the 17O NMR line width of glycine, alanine, proline, leucine, histidine and phenylalanine were investigated at pH 2, 7 and 12.5. The observed viscosity/temperature (η/T) dependence of the reorientation correlation time, τc, is compared with that given by hydrodynamic models. It was found that for amino acids the Gierer–Wirtz model is superior to the Stokes–Einstein–Debye and Hu–Zwanzig models. The 17O quadrupole coupling constant for glycine, alanine and histidine was determined in water solution; the activation energies for molecular tumbling were evaluated, and the hydration of the amino acids in their cationic zwitterionic and anionic ionization states is discussed.

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