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Related Concept Videos

Enzyme Kinetics01:19

Enzyme Kinetics

80.7K
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.
Scientists typically study enzyme kinetics with a fixed amount of enzyme in the controlled environment of a test tube. When more reactant, or substrate, is...
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Introduction to Enzyme Kinetics01:19

Introduction to Enzyme Kinetics

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Enzyme kinetics studies the rates of biochemical reactions. Scientists monitor the reaction rates for a particular enzymatic reaction at various substrate concentrations. Additional trials with inhibitors or other molecules that affect the reaction rate may also be performed.
The experimenter can then plot the initial reaction rate or velocity (Vo) of a given trial against the substrate concentration ([S]) to obtain a graph of the reaction properties. For many enzymatic reactions involving a...
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Protein Dynamics in Living Cells01:19

Protein Dynamics in Living Cells

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Different fluorescence-based techniques are used to study the protein dynamics in living cells. These techniques include FRAP, FRET, and PET.
Fluorescent recovery after photobleaching (FRAP) is a fluorescent-protein-based detection technique used to quantify protein movement rates within the cell. This method exposes a small portion of the cell to an intense laser beam. The laser beam causes permanent photobleaching of the fluorophore-tagged proteins in the exposed region. As the bleached...
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Determination of In Vitro and Cellular Turn-on Kinetics for Fluorogenic RNA Aptamers
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Determination of In Vitro and Cellular Turn-on Kinetics for Fluorogenic RNA Aptamers

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Single-enzyme kinetics with fluorogenic substrates: lessons learnt and future directions.

Petri Turunen1, Alan E Rowan1, Kerstin Blank1

  • 1Radboud University Nijmegen, Institute for Molecules and Materials, Department of Molecular Materials, Heyendaalseweg 135, 6525 AJ Nijmegen, The Netherlands.

FEBS Letters
|June 17, 2014
PubMed
Summary
This summary is machine-generated.

Single-molecule fluorescence enables real-time enzyme kinetics studies. Improving fluorogenic substrates and using nanophotonic detection enhance signal-to-noise for accurate single-enzyme analysis.

Keywords:
Enzyme dynamicsEnzyme kineticsFluorogenic substrateNanophotonic structureSingle-molecule fluorescenceZero mode waveguide

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Area of Science:

  • Biochemistry
  • Biophysics
  • Analytical Chemistry

Background:

  • Single-molecule fluorescence techniques offer high resolution for biological reaction kinetics.
  • Fluorogenic substrates allow real-time observation of enzymatic reactions with single-turnover resolution.

Purpose of the Study:

  • To review the current state of single-molecule fluorescence for enzyme kinetics.
  • To discuss limitations including substrate stoichiometry and signal-to-noise ratio.
  • To present advancements in fluorogenic substrates and nanophotonic detection schemes.

Main Methods:

  • Utilizing fluorogenic substrates to monitor enzymatic reactions at the single-molecule level.
  • Analyzing kinetic information from turnover sequences to understand reaction substeps.
  • Employing nanophotonic structures like zero-mode waveguides and nanoantennas for enhanced detection.

Main Results:

  • Current methods are limited by substrate stoichiometry and signal-to-noise ratio.
  • Nanophotonic approaches effectively reduce detection volume, boosting signal-to-noise.
  • Improvements in substrates and detection are crucial for accurate single-enzyme studies.

Conclusions:

  • Advancements in fluorogenic substrates and nanophotonic detection are key to overcoming current limitations.
  • These combined strategies will enable precise single-enzyme experiments under biologically relevant conditions.