Abstract
A proton magnetic resonance and relaxation study has been carried out in the solid state on 10 of the 20 amino acids encountered in proteins, namely alanine, arginine, aspartic acid, glutamine, glycine, isoleucine, leucine, methionine, serine, and valine. In all cases a relaxation minimum attributed to reorientation of the NH 3 group was found. Additional minima were observed at lower temperatures in the amino acids which have methyl groups in their side chains. Correlation times, activation energies, and frequency factors characterizing each motional process have been extracted and are compared. A single-crystal proton magnetic resonance study of partially deuterated a-glycine, D 3N +-CH 2COO −,, has also been carried out. The spectra obtained by Fourier transformation of the free induction decays consisted of four lines which yielded accurate structural information concerning the methylene group.
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