Protein sequence determination.

more than 50 years of sequencing, but progress has been slow at first. Initially, efforts were made to establish separation techniques for
proteins
and
peptides
and to determine the type and content of their
amino acids
. Before 1945, there was no method of quantitative determination of protein sequences. Over the next decade, with the rapid development of
chromatography
technology and marking methods, the first full sequence determination of the peptide
hormone
(insulin) was completed in 1955 (Ryle, etc., 1955). Five years later, the first sequence determination of

(Hirs, etc., 1960) was completed. In 1965, about 20 protein sequences containing more than 100 residues were identified. By 1980, that number had reached 1,500. Today, 300,000 protein sequences have been sequenced, which was unthinkable 50 years ago.
, protein sequence determination was mainly done using the manual Edman degradation and Edman deglation -dansylation method (Edman, 1950). The rapid progress of protein sequence determination is due to the success of automatic sequencer. The automatic sequencing instrument, which began in 1980, is nearly 10,000 times more sensitive than the sequencing method invented by Edelman and Begg in 1967.development of
technology has opened up a new way for protein sequence assay. The first time complete protein molecules were measured in this way was in 1997. The outstanding advantage of mass spectrometry sequencing is that special amino acids obtained from post-translation modification can be identified. This modification information is not available when protein sequence determination is performed by other methods. It is by using mass spectrometry that important conclusions have been drawn that g-amino butyric acid is at the end of coagulation N-. .