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Determination of dynamic parameters in amino acids from 17 O NMR line width measurements
Author(s) -
TrittGoc J.,
Fiat D.
Publication year - 1991
Publication title -
magnetic resonance in chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.483
H-Index - 72
eISSN - 1097-458X
pISSN - 0749-1581
DOI - 10.1002/mrc.1260290212
Subject(s) - chemistry , alanine , amino acid , histidine , quadrupole , glycine , proton nmr , phenylalanine , coupling constant , viscosity , line width , cationic polymerization , proton , analytical chemistry (journal) , stereochemistry , computational chemistry , thermodynamics , organic chemistry , atomic physics , biochemistry , physics , optics , particle physics , quantum mechanics
The viscosity and temperature dependence of the 17 O 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, τ c , 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 17 O 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.