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首页> 外文期刊>Journal of Molecular Biology >Structure of the transition state in the folding process of human procarboxypeptidase A2 activation domain
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Structure of the transition state in the folding process of human procarboxypeptidase A2 activation domain

机译：人羧肽酶A2激活域折叠过程中过渡态的结构

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The transition state for the folding pathway of the activation domain of human procarboxypeptidase A2 (ADA2h) has been analyzed by the protein engineering approach. Recombinant ADA2h is an 81-residue globular domain with no disulfide bridges or cis-prolyl bonds, which follows a two-state folding transition. Its native fold is arranged in two alpha-helices packing against a four-stranded beta-sheet. Application of the protein engineering analysis for 20 single-point mutants spread throughout the whole sequence indicates that the transition state for this molecule is quite compact, possessing some secondary structure and a hydrophobic core in the process of being consolidated. The core (folding nucleus) is made by the packing of alpha-helix 2 and the two central beta-strands. The other two strands, at the edges of the beta-sheet, and alpha-helix 1 seem to be completely unfolded. These results, together with previous analysis of ADA2h with either of its two alpha-helices stabilized through improved local interactions, suggest that alpha-helix 1 does not contribute to the folding nucleus, even though it is partially folded in the denatured state under native conditions. On the other hand, alpha-helix 2 folds partly in the transition state and is part of the folding nucleus. It is suggested that a good strategy to improve folding speed in proteins would be to stabilize the helices that are not folded in the denatured state but are partly present in the transition state. Comparison with other proteins shows that there is no clear relationship between fold and/or size with folding speed and level of structure in the transition state of proteins. (C) 1998 Academic Press. [References: 39]
机译：已通过蛋白质工程方法分析了人羧肽酶原A2（ADA2h）激活域折叠路径的过渡态。重组ADA2h是一个81位残基的球状结构域，没有二硫键或顺-脯氨酰键，该结构遵循两个状态的折叠过渡。它的天然褶皱排列成两个α螺旋，紧靠四链β-折叠。对遍布整个序列的20个单点突变体进行蛋白质工程分析的应用表明，该分子的过渡态非常紧凑，在巩固过程中具有一些二级结构和疏水核。核心（折叠核）是由α-螺旋2和两个中央β链的堆积形成的。在β-折叠边缘的其他两条链和α-螺旋1似乎已完全展开。这些结果，以及先前对ADA2h的两个α螺旋通过改善局部相互作用而稳定化的分析表明，即使在自然条件下以变性状态将其部分折叠，α-螺旋1也不会对折叠核做出贡献。 。另一方面，α-螺旋2在过渡状态中部分折叠，并且是折叠核的一部分。建议提高蛋白质折叠速度的好策略是稳定未在变性状态折叠但部分以过渡状态存在的螺旋。与其他蛋白质的比较表明，在蛋白质的过渡态中，折叠和/或大小与折叠速度和结构水平之间没有明确的关系。 （C）1998年学术出版社。 [参考：39]

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