β-Barrel proteins from bacterial outer membranes:: structure, function and refolding
β-Barrel proteins from bacterial outer membranes:: structure, function and refolding
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DOI：
10.1016/s0959-440x(99)80064-5
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发表时间：
1999-08-01
影响因子：
6.8
通讯作者：
Buchanan, SK
中科院分区：
文献类型：
--
作者：
Buchanan, SK
最近解决的外膜蛋白结构包括已知的最小和最大的β-桶结构，其功能不同于一般和特定的孔蛋白。在外膜中表达的蛋白质和作为细胞质聚集体沉积的蛋白质都已用于结构测定。由于大多数β-桶蛋白可以以聚集形式（包涵体）过表达并重折叠至天然状态，这提供了膜靶向表达策略的替代方案，并产生足够量的蛋白质用于未来的结构研究。
Recently solved outer membrane protein structures include the smallest and largest known beta-barrel structures, with functions distinct from the general and specific porins. Both protein expressed in outer membranes and protein deposited as cytoplasmic aggregates have been used for the structure determinations. As most beta-barrel proteins can be overexpressed in an aggregated form (inclusion bodies) and refolded to the native state, this provides an alternative to membrane-targeted expression strategies and yields sufficient quantities of protein for future structural studies.