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α-螺旋膜蛋白的体外折叠

In vitro folding of alpha-helical membrane proteins.

作者信息

Kiefer Hans

机构信息

m-phasys GmbH, Vor dem Kreuzberg 17, D-72070 Tübingen, Germany.

出版信息

Biochim Biophys Acta. 2003 Feb 17;1610(1):57-62. doi: 10.1016/s0005-2736(02)00717-4.

DOI:10.1016/s0005-2736(02)00717-4
PMID:12586380
Abstract

For large-scale production, as required in structural biology, membrane proteins can be expressed in an insoluble form as inclusion bodies and be refolded in vitro. This requires refolding conditions where the native form is thermodynamically stable and where nonproductive pathways leading to aggregation are avoided. Examples of successful refolding are reviewed and general guidelines to establish refolding protocols of membrane proteins are presented.

摘要

对于结构生物学中所需的大规模生产,膜蛋白可以以不溶性形式作为包涵体表达,并在体外进行重折叠。这需要重折叠条件,即天然形式在热力学上是稳定的,并且避免导致聚集的非生产性途径。本文综述了成功重折叠的实例,并给出了建立膜蛋白重折叠方案的一般指导原则。

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