PRINCIPLES THAT GOVERN FOLDING OF PROTEIN CHAINS
PRINCIPLES THAT GOVERN FOLDING OF PROTEIN CHAINS
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DOI：
10.1126/science.181.4096.223
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发表时间：
1973-01-01
期刊：
影响因子：
56.9
通讯作者：
ANFINSEN, CB
中科院分区：
文献类型：
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作者：
ANFINSEN, CB
我从瑞典皇家科学院收到的电报“.核糖核酸酶的研究，特别是氨基酸序列和生物活性构象之间的关系。“我和我的同事们对控制多肽链折叠成蛋白质独特三维结构的过程的性质所做的工作确实受到核糖核酸酶分子观察的强烈影响。其他许多人，包括安森和米尔斯基（1）在20世纪30年代和Lumry和Eyring（2）在20世纪50年代，观察和讨论了蛋白质变性的可逆性。然而，自然选择的这一结果的真正优雅性被核糖核酸酶的工作戏剧化了，因为该分子在通过还原切割其四个二硫键（图1）完全变性后的重新折叠，只需要105种可能的配对中的1种。
The telegranl that I received from the Swedish Royal Academy of Sciences sp· ecifically cites'"... studies on ribonuclease, in particular the relationship between the amino acid sequence and the biologically active conformation...." The work that my colleagues and I have carried out on the nature of the process that controls the folding of polypeptide chains into the unique three-dimensional structures of proteins was, indeed, strongly influenced by observations on the ribonuclease molecule. Many others, including Anson and Mirsky (1) in the 1930's and Lumry and Eyring (2) in the 1950's, had observed and discussed the reversibiIi~'Y of denaturation of proteins. However, the true elegance of this consequence of natural selection was dramatized by the ribonuclease work, since the refolding of this molecule, after full denaturation by reductive cleavage of its four disulfide bonds (Fig. 1), required that only 1 of the 105 possible pairings of