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- W2896985933 abstract "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." @default.
- W2896985933 created "2018-10-26" @default.
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- W2896985933 date "2018-10-20" @default.
- W2896985933 modified "2023-10-03" @default.
- W2896985933 title "Constructing Kinetically Controlled Denaturation Isotherms of Folded Proteins Using Denaturant-Pulse Chaperonin Binding" @default.
- W2896985933 cites W2010370535 @default.
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- W2896985933 doi "https://doi.org/10.1007/978-1-4939-8820-4_19" @default.
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