Cordes M H, Davidson A R, Sauer R T
Department of Biology, Massachusetts Institute of Technology, Cambridge 02139, USA.
Curr Opin Struct Biol. 1996 Feb;6(1):3-10. doi: 10.1016/s0959-440x(96)80088-1.
Protein design efforts are beginning to yield molecules with many of the properties of natural proteins. Such experiments are informed by and contribute to our understanding of the sequence determinants of protein folding and stability. The most important design elements seem to be the proper placement of hydrophobic residues along the polypeptide chain and the ability of these residues to form a well packed core. Buried polar interactions, turn and capping motifs and secondary structural propensities also contribute, although probably to a lesser extent.
蛋白质设计工作开始产生具有许多天然蛋白质特性的分子。此类实验为我们对蛋白质折叠和稳定性的序列决定因素的理解提供了依据，并有助于这一理解。最重要的设计要素似乎是疏水残基在多肽链上的恰当排布，以及这些残基形成紧密堆积核心的能力。埋藏的极性相互作用、转角和封端基序以及二级结构倾向也有作用，尽管可能程度较小。
