The chemical synthesis of proteins
The chemical synthesis of proteins
复制标题
蛋白质的化学合成
DOI：
10.1002/pro.5560050925
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发表时间：
1996
期刊：
影响因子：
8
通讯作者：
B. Merrifield
中科院分区：
文献类型：
--
作者：
B. Merrifield
In 1942 I enrolled in the biochemistry class at UCLA, being taught by Professor Max Dunn, and was introduced into the world of amino acids, peptides, and proteins. The amino acids had been well studied and much was also known about proteins, but no complete amino acid composition was yet known and a sequence of even a small protein was still 9 years away. The idea of a chemical synthesis of a protein was not even discussed. My eventual entry into this field was a gradual process that, in the beginning, was completely unplanned but later became a serious goal. On returning to graduate school 2 years later I served as laboratory assistant in the biochemistry course and began my graduate studies with Dr. Dunn. He was well known for his amino acid syntheses, and his laboratory provided the only source in the world of all of the natural amino acids in highly purified form. They were aptly characterized in a current magazine article as “worth their weight in gold.” Dunn (Dunn et al., 1944) had just introduced microbiological methods for the quantitative assay of amino acids, and I joined his group to continue that work. This was the only rapid general method for amino acid analysis and greatly stimulated and accelerated studies on proteins. The chromatographic methods of Moore and Stein had still not been developed. By 1948 I had extended this microbiological approach to the pyrimidines, for which there was no satisfactory analytical method. I was able to determine that cytosine and uracil were not in equimolar ratio, 0.71, in RNA, and cytosine and thymine were not equimolar, 0.6 1, in thymus DNA. Unfortunately, I did not have the purine data that would have led to U/A and C/G ratios. The dangers of developing new analytical methods soon became apparent to me when Chargaff’s chromatographic techniques did give these ratios
