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 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.
authors: Department of Chemistry, University of Illinois, Urbana-Champaign, IL, USA.
authors: Apratim
authors: A
authors: Dhar
authors: Maxim
authors: M
authors: Prigozhin
authors: Hannah
authors: H
authors: Gelman
authors: Martin
authors: M
authors: Gruebele
mesh_terms: D000465:Algorithms; D045744:Cell Line, Tumor; D002846:Chromatography, Affinity; D003627:Data Interpretation, Statistical; D004926:Escherichia coli; D031541:Fluorescence Resonance Energy Transfer; D006801:Humans; D007091:Image Processing, Computer-Assisted; D007700:Kinetics; D011487:Protein Conformation; D011489:Protein Denaturation; D055550:Protein Stability; D059010:Single-Cell Analysis; D012984:Software; D013816:Thermodynamics; D014162:Transfection; D051844:alpha-Synuclein / Q000096:biosynthesis / Q000737:chemistry* / Q000302:isolation & purification
chemical_list: D051844:alpha-Synuclein