CHARACTERIZATION OF A HELICAL PROTEIN DESIGNED FROM 1ST PRINCIPLES
CHARACTERIZATION OF A HELICAL PROTEIN DESIGNED FROM 1ST PRINCIPLES
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DOI：
10.1126/science.3043666
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发表时间：
1988-08-19
期刊：
影响因子：
56.9
通讯作者：
DEGRADO, WF
中科院分区：
文献类型：
--
作者：
REGAN, L;DEGRADO, WF
蛋白质的一级氨基酸序列如何决定其三维结构的问题仍然没有答案。解决这一问题的一种方法是从头设计模型肽和蛋白质，使其具有所需的三维结构。一个系统的方法，旨在设计一个四螺旋束蛋白。合成了编码设计蛋白的基因，并在大肠杆菌中表达了该蛋白，并纯化至均一。该蛋白被证明是单体，高度螺旋，非常稳定的盐酸胍（GuHCl）变性。因此，已经设计了一种能够在水溶液中采用稳定的折叠结构的球状蛋白。
The question of how the primary amino acid sequence of a protein determines its three-dimensional structure is still unanswered. One approach to this problem involves the de novo design of model peptides and proteins that should adopt desired three-dimensional structues. A systematic approach was aimed at the design of a four-helix bundle protein. The gene encoding the designed protein was synthesized and the protein was expressed in Escherichia coli and purified to homogeneity. The protein was shown to be monomeric, highly helical, and very stable to denaturation by guanidine hydrochloride (GuHCl). Thus a globular protein has been designed that is capable of adopting a stable, folded structure in aqueous solution.