@inbook{ee518270c72d490589aa03f12ec2dd0b,
title = "Studying IDP stability and dynamics by fast relaxation imaging in living cells",
abstract = "Fast relaxation imaging (FReI) temperature-tunes living cells and applies small temperature jumps to them, to monitor biomolecular stability and kinetics in vivo. The folding or aggregation state of a target protein is monitored by F{\"o}rster resonance energy transfer (FRET). Intrinsically disordered proteins near the structured-unstructured boundary are particularly sensitive to their environment. We describe, using the IDP α-synuclein as an example, how FReI can be used to measure IDP stability and folding inside the cell.",
keywords = "Fluorescence, Folding kinetics, Folding thermodynamics, In vivo, Intrinsically disordered protein, Temperature jump, Thermal denaturation",
author = "Apratim Dhar and Maxim Prigozhin and Hannah Gelman and Martin Gruebele",
year = "2012",
doi = "10.1007/978-1-61779-927-3_8",
language = "English (US)",
isbn = "9781617799266",
series = "Methods in Molecular Biology",
pages = "101--111",
editor = "Vladimir Uversky and Vladimir Uversky and Keith Dunker",
booktitle = "Intrinsically Disordered Protein Analysis",
}