The first mass spectrometric study on proteins, using GC-MS, was reported by Biemann in 1975. It was shown that the complete sequence analysis of a protein can be achieved by mass spectrometry. After his initial work, the development of fast atom bombardment and 4 sector instrumentation facilitated not only the complete sequence of a protein but also top-down proteomics and studies of protein interactions. Remarkable progress has been made in this field as the result of the development of ESI and MALDI instruments. Consequently, studies of the tertiary structure and the surface structure of a protein can now be achieved by mass spectrometry with a small amount of sample. This paper discusses the characterization, not only the primary structure, but also the tertiary structure of proteins via the use of mass spectrometry.
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