Method Article

Assessing Bacterial Chaperone Activity via Thermal Unfolding of a Model Protein

November 28th, 2025

In This Article

Abstract

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Source: Dahl, J. et al. Detection of the pH-dependent Activity of Escherichia coli Chaperone HdeB In Vitro and In Vivo. J. Vis. Exp. (2016)

This video demonstrates a fluorescence spectrophotometer-based assay to evaluate chaperone activity on a substrate protein under acid and heat stress. It outlines the steps for monitoring substrate unfolding and aggregation through light scattering, comparing conditions with and without the chaperone.

Protocol

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1. Chaperone Activity Assay Using Thermally Unfolding Malate Dehydrogenase (MDH)

NOTE: The influence of purified HdeB on the aggregation of thermally unfolding porcine mitochondrial malate dehydrogenase (MDH) at different pH values was monitored as described below. All listed protein concentrations refer to the monomer concentration.

  1. To prepare MDH, dialyze MDH at 4 °C overnight against 4 L buffer C (50 mM potassium phosphate, 50 mM sodium chloride (NaCl), pH 7.5) and concentrate the protein to approximately 100 µM using centrifugal filter units with a molecular weight cut-off of 30 kDa.
    NOTE: Careful dialysis of MDH is required as MDH is delivered as an ammonium sulfate solution.
  2. To remove aggregates, centrifuge the protein for 20 min at 20,000 x g at 4 °C. Determine MDH concentration by absorbance at 280 nm (ε280 nm= 7,950 M-1 cm-1). Prepare 50 µl aliquots of MDH and flash-freeze the aliquots for storage.
  3. Place a 1 ml quartz cuvette into a fluorescence spectrophotometer equipped with temperature-controlled sample holders and stirrers. Set λex/em to 350 nm.
  4. Add appropriate volumes of pre-warmed (43 °C) buffer D (150 mM potassium phosphate, 150 mM NaCl) at the desired pH values (here: pH 2.0, pH 3.0, pH 4.0, and pH 5.0) to the cuvette and set the temperature in the cuvette holder to 43 °C. The total volume is 1,000 µl.
  5. Add 12.5 µM HdeB (or alternatively, the same volume of HdeB storage buffer for the buffer control) to the buffer, followed by the addition of 0.5 µM MDH. Begin monitoring light scattering. Incubate the reaction for 360 sec to allow sufficient unfolding of MDH.
  6. Raise the pH to 7 by adding 0.16-0.34 volume of 2 M unbuffered K2HPO4 and continue recording light scattering for another 440 sec.
  7. Set the extent of MDH aggregation that is recorded in the absence of the chaperone at a defined time point after neutralization (hereafter 500 sec, when the maximal light scattering of MDH was observed) to 100%. Normalize HdeB's activity to the light scattering signal of MDH in the absence of HdeB at each indicated pH value.

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Materials

List of materials used in this article
NameCompanyCatalog NumberComments
Malate dehydrogenase (MDH)Roche10127914001
Potassium phosphate (Monobasic)Fisher ScientificBP362-500
Potassium phosphate (Dibasic)Fisher ScientificBP363-1
F-4500 fluorescence spectrophotometerHitachiFL25
Fluorescence Cell cuvetteHellma Analytics119004F-10-40
Hydrochloric AcidFisher ScientificA144-212
Sodium HydroxideFisher ScientificBP359-500
Amicon Ultra Centrifugal Filter Units 30KMilliporeUFC803024
Sodium chlorideFisher ScientificS271-10
Spectra/Por 1 Dialysis Membrane MWCO: 6 kDaSpectrum Laboratories132650
Varian Cary 50 spectrophotometerAgilent Tech

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Tags

Fluorescence SpectrophotometerLight ScatteringSubstrate ProteinAcid StresspH DependentEscherichia coliHdeB ChaperoneMDH Substrate

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