Expanding heme-protein folding space using designed multi-heme β-sheet mini-proteins
Expanding heme-protein folding space using designed multi-heme β-sheet mini-proteins
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DOI：
10.1038/s42004-018-0078-z
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发表时间：
2018-11-05
影响因子：
5.9
通讯作者：
Bhattacharjya, Surajit
中科院分区：
文献类型：
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作者：
D'Souza, Areetha;Torres, Jaume;Bhattacharjya, Surajit
大自然主要利用螺旋蛋白而不是β-折叠来进行血红素/多血红素协调。对血红素蛋白质结构的了解激发了利用卷曲螺旋结构设计血红素蛋白质。相比之下，从头设计的β-折叠蛋白不太成功。然而，设计具有编码特定功能的离散折叠 β-折叠结构的蛋白质对于开发新的合成分子（例如合成分子）具有巨大潜力。酶、抑制剂。在这里，我们报告了多血红素结合四链、六链、八链和十二链β-折叠微型蛋白的设计和表征（
Nature has primarily exploited helical proteins, over beta-sheets, for heme/multi-heme coordination. Understating of heme-protein structures has motivated the design of heme proteins utilizing coiled-coil helical structure. By contrast, de novo designed beta-sheet proteins are less successful. However, designing proteins with discretely folded beta-sheet structures encoding specific functions would have great potential for the development of new synthetic molecules e.g. enzymes, inhibitors. Here we report the design and characterization of multi-heme binding four-, six-, eight-, and twelve-stranded beta-sheet mini-proteins (