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O'Neil PT, Machen AJ, Thompson JA, Wang W, Hoang QQ, Baldwin MR, Khar KR, Karanicolas J, Fisher MT
Constructing Kinetically Controlled Denaturation Isotherms of Folded Proteins Using Denaturant-Pulse Chaperonin Binding
Methods Mol Biol (2019) 1873:293-304.
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.
Note
Publication Date: 2019-01-01.
PMCID: PMC6196737
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Last updated on Monday, November 04, 2019