Abstract
We have obtained IOO-MHz high-resolution proton magnetic resonance (pmI') spectra of gelatin solutions and gels under a variety of conditions. An analysis of these narrow-line spcctra in term of contributions from individual amino acid residue types has resulted in the assignment of all the principal spectral peaks. A computer program that sums individual subspectra from model systems (polypeptides, homopolyamino acids, amino acids, etc.) has enabled nearly quantitative curve resolution involving all the major amino acid constituents. In certain cases (e.g., arginine) good quantitative analysis can be made rapidly by pmI'. The poll' spectra of concentrated, rigid gels show considerable high-resolution intensity, observable even after 18 hours of equilibration at. A gradual increase of pmI' intensity accompanies increase in temperature and gives a sigmoidal curve of intensity vs. temperature. The data are discussed in terms of thc isola table "nongelling" component of gelatin.

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