由互补RNA所指定的肽的结合。
Binding of peptides that are specified by complementary RNAs.
作者信息
Blalock J E, Bost K L
出版信息
Biochem J. 1986 Mar 15;234(3):679-83. doi: 10.1042/bj2340679.
Abstract
An interesting pattern in the genetic code was reported previously [Blalock & Smith (1984) Biochem. Biophys. Res. Commun. 121, 203-207]. In the 5'-to-3' direction, codons for hydrophilic and hydrophobic amino acids are generally complemented by codons for hydrophobic and hydrophilic amino acids respectively. The average tendency of codons for 'unchanged' (slightly hydrophilic) amino acids was to be complemented by codons for 'unchanged' amino acids. We now show that the same pattern results when the complementary codon is read in the 3'-to-5' direction. This pattern is further shown to result in the interaction of peptides specified by complementary RNAs regardless of whether the amino acids are assigned in the 5'-to-3' or the 3'-to-5' direction. Here we demonstrate that peptides specified by complementary RNAs bind to each other with specificity and high affinity.
摘要
先前曾报道过遗传密码中的一种有趣模式[布莱洛克和史密斯（1984年），《生物化学与生物物理学研究通讯》，第121卷，203 - 207页]。在5'至3'方向上，亲水性和疏水性氨基酸的密码子通常分别由疏水性和亲水性氨基酸的密码子互补。“不变”（略具亲水性）氨基酸的密码子的平均趋势是由“不变”氨基酸的密码子互补。我们现在表明，当互补密码子从3'至5'方向读取时，会产生相同的模式。进一步表明，这种模式会导致互补RNA所指定的肽段相互作用，而不管氨基酸是按5'至3'方向还是3'至5'方向分配。在此我们证明，互补RNA所指定的肽段以特异性和高亲和力相互结合。
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