Constructing Kinetically Controlled Denaturation Isotherms of Folded Proteins Using Denaturant-Pulse Chaperonin Binding.
Constructing Kinetically Controlled Denaturation Isotherms of Folded Proteins Using Denaturant-Pulse Chaperonin Binding.
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使用变性剂脉冲伴侣蛋白结合构建折叠蛋白的动力学控制变性等温线。
DOI：
10.1007/978-1-4939-8820-4_19
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发表时间：
2019
期刊：
影响因子：
--
通讯作者：
Fisher,MarkT
中科院分区：
文献类型：
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作者：
O'Neil,PierceT;Machen,AlexandraJ;Thompson,JackieA;Wang,Wei;Hoang,QuyenQ;Baldwin,MichaelR;Khar,KarenR;Karanicolas,John;Fisher,MarkT
评估蛋白质动力学稳定性的方法，特别是那些易于聚集的蛋白质，对于建立配体诱导的稳定作用非常有用。由于易于聚集的蛋白质本质上难以使用，因此大多数基于溶液的方法都会受到这种固有不稳定性的影响。在这里，我们描述了一种无标记方法，该方法检查固定蛋白的变性，其中通过伴侣蛋白结合捕获和检测动态未折叠蛋白群体。
Methods to assess the kinetic stability of proteins, particularly those that are aggregation prone, are very useful in establishing ligand induced stabilizing effects. Because aggregation prone proteins are by nature difficult to work with, most solution based methods are compromised by this inherent instability. Here, we describe a label-free method that examines the denaturation of immobilized proteins where the dynamic unfolded protein populations are captured and detected by chaperonin binding.