Studying IDP stability and dynamics by fast relaxation imaging in living cells

Apratim Dhar, Maxim Prigozhin, Hannah Gelman, Martin Gruebele

Research output: Chapter in Book/Report/Conference proceedingChapter

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 Förster 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.

Original languageEnglish (US)
Title of host publicationIntrinsically Disordered Protein Analysis
Subtitle of host publicationVolume 1, Methods and Experimental Tools
EditorsVladimir Uversky, Vladimir Uversky, Keith Dunker
Pages101-111
Number of pages11
DOIs
StatePublished - Aug 29 2012

Publication series

NameMethods in Molecular Biology
Volume895
ISSN (Print)1064-3745

Keywords

  • Fluorescence
  • Folding kinetics
  • Folding thermodynamics
  • In vivo
  • Intrinsically disordered protein
  • Temperature jump
  • Thermal denaturation

ASJC Scopus subject areas

  • Molecular Biology
  • Genetics

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  • Cite this

    Dhar, A., Prigozhin, M., Gelman, H., & Gruebele, M. (2012). Studying IDP stability and dynamics by fast relaxation imaging in living cells. In V. Uversky, V. Uversky, & K. Dunker (Eds.), Intrinsically Disordered Protein Analysis: Volume 1, Methods and Experimental Tools (pp. 101-111). (Methods in Molecular Biology; Vol. 895). https://doi.org/10.1007/978-1-61779-927-3_8