Sauer R T
Department of Biology, Massachusetts Institute of Technology, Cambridge 02139-4307, USA.
Fold Des. 1996;1(2):R27-30. doi: 10.1016/S1359-0278(96)00015-6.
Combinatorial mutagenesis experiments show the existence of many different solutions to the problem of complementary packing of non-polar sidechains in the protein core. They suggest that a significant amount of structural information is carried by the simple pattern of polar and non-polar residues along the polypeptide chain, indicate that the formation of buried polar interactions may be a fundamentally slow step in protein folding and show that proteins with many native properties occur at reasonable frequencies in random sequence libraries.
组合诱变实验表明，在蛋白质核心中，非极性侧链的互补堆积问题存在许多不同的解决方案。这些实验表明，沿着多肽链的极性和非极性残基的简单模式携带了大量的结构信息，表明埋藏的极性相互作用的形成可能是蛋白质折叠中一个从根本上来说缓慢的步骤，并表明具有许多天然特性的蛋白质在随机序列文库中以合理的频率出现。
