@inbook{3cc5426f54424604b0b6fc78a48d617f,
title = "Constructing kinetically controlled denaturation isotherms of folded proteins using denaturant-pulse chaperonin binding",
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.",
keywords = "Aggregation, Biolayer interferometry, Chaperonin, Denaturant pulse, Denaturation, GroEL, Protein folding",
author = "O{\textquoteright}Neil, {Pierce T.} and Machen, {Alexandra J.} and Thompson, {Jackie A.} and Wei Wang and Hoang, {Quyen Q.} and Baldwin, {Michael R.} and Khar, {Karen R.} and John Karanicolas and Fisher, {Mark T.}",
note = "Publisher Copyright: {\textcopyright} 2019, Springer Science+Business Media, LLC, part of Springer Nature.",
year = "2019",
doi = "10.1007/978-1-4939-8820-4_19",
language = "English",
volume = "1873",
series = "Methods in molecular biology (Clifton, N.J.)",
publisher = "Humana Press Inc.",
pages = "293--304",
booktitle = "Methods in Molecular Biology",
address = "United States",
}