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Related Concept Videos

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Kinetic energy is the ability of an object in motion to do work or enact change. It can take on many forms. For instance, water flowing down a waterfall has kinetic energy. In biological systems, particles of light travel and are absorbed by plants to create chemical energy. Animals consume the chemical energy and give off molecules that carry their scent through the air. They also generate kinetic energy when they run away from predators. Entire systems also possess kinetic energy, like the...
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Enzymes speed up reactions by lowering the activation energy of the reactants. The speed at which the enzyme turns reactants into products is called the rate of reaction. Several factors impact the rate of reaction, including the number of available reactants. Enzyme kinetics is the study of how an enzyme changes the rate of a reaction.
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Consider a truck trying to pull a stationary car. As the truck exerts a force on the car, static friction is created at the point of contact between the two surfaces. This frictional force resists the car's movement and keeps it at rest. However, when the applied force by the truck surpasses the limiting static frictional force, an interesting phenomenon occurs. The frictional force at the interface reduces to a lower value, known as the kinetic frictional force. At this point, the car...
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It’s plausible to suppose that the greater the velocity of a body, the greater effect it could have on other bodies. This does not depend on the direction of the velocity, only its magnitude. At the end of the seventeenth century, a quantity was introduced into mechanics to explain collisions between two perfectly elastic bodies, in which one body makes a head-on collision with an identical body at rest. When they collide, the first body stops, and the second body moves off with the...
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Use of Label-free Optical Biosensors to Detect Modulation of Potassium Channels by G-protein Coupled Receptors
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Evaluation of Kinetics Using Label-Free Optical Biosensors.

Yung-Shin Sun1, James P Landry2, X D Zhu2

  • 1Department of Physics, Fu-Jen Catholic University, New Taipei City, Taiwan.

Instrumentation Science & Technology
|March 26, 2019
PubMed
Summary
This summary is machine-generated.

Sophisticated models are essential for accurately analyzing biomolecular interactions using optical biosensors. A one-to-two binding model better fits real-time kinetic data than a simple one-to-one model, accounting for surface complexities.

Keywords:
Langmuir equationbiomolecular interactionlabel-free optical biosensoroblique-incidence reflectivity difference (OI-RD) microscopyreaction rates

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Area of Science:

  • Biomolecular Interaction Analysis
  • Surface Plasmon Resonance (SPR) Biosensing
  • Biophysical Chemistry

Background:

  • Optical biosensors offer label-free, real-time analysis of biomolecular binding kinetics.
  • Surface-based biosensing methods can be complicated by mass transport and immobilization heterogeneity.
  • Standard kinetic analysis often uses the one-to-one Langmuir model.

Purpose of the Study:

  • To evaluate the fitting accuracy of different kinetic models for optical biosensor data.
  • To investigate the impact of surface effects on biomolecular interaction analysis.
  • To determine the optimal model for interpreting antibody-antigen binding curves.

Main Methods:

  • Utilized an ellipsometry-based optical biosensor to measure real-time binding curves.
  • Acquired kinetic data for various antibody-antigen interactions.
  • Fitted the experimental data to both a one-to-one and a more sophisticated one-to-two binding model.

Main Results:

  • The one-to-two binding model demonstrated a significantly better fit to the experimental kinetic curves compared to the one-to-one model.
  • The improved fit suggests the presence of multiple binding configurations or sites on the immobilized surface.
  • Surface-related issues like immobilization heterogeneity influence kinetic data interpretation.

Conclusions:

  • Simple one-to-one models are often insufficient for accurately describing biomolecular interactions in optical biosensors.
  • More complex models are necessary to account for surface phenomena such as immobilization heterogeneity and mass transport.
  • Accurate kinetic analysis requires models that reflect the complexities of surface-based binding events.