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The current state of methodology for protein sequence analysis is discussed with reference to the enzyme dihydrofolate reductase. Studies on biologically active compounds of unusual structure are shown, covering data on peptide hormones and factor X, the zymogen of a serine protease involved in blood coagulation. Recent research on glycopeptides from biological sources illustrates the development of chemical and mass spectrometric methods for concurrent determination of saccharide and peptide structure. Details of future trends are discussed by reference to present work in the areas of negative chemical ionization, computerized automation and high-field magnet studies.
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Howard R. Morris (1979) studied this question.
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