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The Equilibrium Binding Constant and Binding Strength02:18

The Equilibrium Binding Constant and Binding Strength

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The equilibrium binding constant (Kb) quantifies the strength of a protein-ligand interaction. Kb can be calculated as follows when the reaction is at equilibrium:
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Calorimetry is a technique used to measure the amount of heat involved in a chemical or physical process or to measure the heat transferred to or from a substance. The heat is exchanged with a calibrated and insulated device called the calorimeter. Calorimetry experiments are based on the assumption that there is no heat exchange between the insulated calorimeter and the external environment. The well-insulated calorimeters prevent the transfer of heat between the calorimeter and its external...
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Calorimeters are useful to determine the heat released or absorbed by a chemical reaction. Coffee cup calorimeters are designed to operate at constant (atmospheric) pressure and are convenient to measure heat flow (or enthalpy change) accompanying processes that occur in solution at constant pressure. A different type of calorimeter that operates at constant volume, colloquially known as a bomb calorimeter, is used to measure the energy produced by reactions that yield large amounts of heat and...
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The equilibrium constant for a reaction is calculated from the equilibrium concentrations (or pressures) of its reactants and products. If these concentrations are known, the calculation simply involves their substitution into the Kc expression.
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The difference between the calculated and experimentally measured masses is known as the mass defect of the atom. In the case of helium-4, the mass defect indicates a “loss” in mass of 4.0331 amu – 4.0026 amu = 0.0305 amu. The loss in mass accompanying the formation of an atom from protons, neutrons, and electrons is due to the conversion of that mass into energy that is evolved as the atom forms. The nuclear binding energy is the energy produced when the atoms’ nucleons are bound...
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Thermal Measurement Techniques in Analytical Microfluidic Devices
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Quantifying Biomolecular Binding Constants using Video Paper Analytical Devices.

Benjamin S Miller1,2, Claudio Parolo1, Valérian Turbé1,2

  • 1London Centre for Nanotechnology, University College London, 17-19 Gordon Street, London, WC1H 0AH, UK.

Chemistry (Weinheim an Der Bergstrasse, Germany)
|May 18, 2018
PubMed
Summary
This summary is machine-generated.

Researchers developed an ultra-low-cost paper microfluidics platform for biochemical analysis. This method quantifies protein binding constants and kinetics using simple video imaging, making advanced diagnostics accessible.

Keywords:
adsorptionnanoparticlespaper-basedprotein-protein interactionssmartphones

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Area of Science:

  • Biochemistry
  • Microfluidics
  • Analytical Chemistry

Background:

  • Traditional biochemical analysis platforms are often expensive and require specialized laboratory equipment.
  • There is a need for accessible and low-cost methods for quantifying protein binding constants and kinetics.

Purpose of the Study:

  • To report a novel, ultra-low-cost biochemical analysis platform using paper microfluidics.
  • To quantify protein dissociation binding constants and kinetics.
  • To demonstrate the platform's utility in resource-limited settings.

Main Methods:

  • Utilizing paper microfluidics combined with video imaging.
  • Employing nanoparticle-antibody conjugates for binding measurements on paper.
  • Applying the Langmuir Adsorption Model to temporal binding data.
  • Measuring antibody-antigen dissociation constants using a smartphone camera.

Main Results:

  • Temporal measurements of nanoparticle-antibody conjugate binding followed the Langmuir Adsorption Model.
  • Dissociation constants measured on paper showed excellent agreement with a gold-standard interferometer.
  • The platform, demonstrated with a smartphone, is 500-fold cheaper than the reference method.
  • The system can be multiplexed to measure ten reactions in parallel.

Conclusions:

  • The paper microfluidics platform offers a low-cost, accessible method for quantitative analytical biochemistry.
  • This technology has broad applications in disease diagnostics, drug discovery, and environmental analysis, particularly in resource-limited settings.
  • The integration of paper, video imaging, and smartphones democratizes advanced biochemical analysis.