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Related Concept Videos

Enzyme Kinetics01:19

Enzyme Kinetics

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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Related Experiment Video

Updated: May 25, 2026

High-Resolution Neutron Spectroscopy to Study Picosecond-Nanosecond Dynamics of Proteins and Hydration Water
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High-Resolution Neutron Spectroscopy to Study Picosecond-Nanosecond Dynamics of Proteins and Hydration Water

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Single-molecule lysozyme dynamics monitored by an electronic circuit.

Yongki Choi1, Issa S Moody, Patrick C Sims

  • 1Institute for Surface and Interface Science, University of California Irvine, Irvine, CA 92697-2375, USA.

Science (New York, N.Y.)
|January 24, 2012
PubMed
Summary
This summary is machine-generated.

Single lysozyme molecule motion was electronically monitored using a carbon nanotube field-effect transistor, revealing its processive enzyme activity and dynamic disorder. This technique overcomes fluorescence limitations for studying protein dynamics.

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Area of Science:

  • Biophysics
  • Biochemistry
  • Nanotechnology

Background:

  • Studying single protein dynamics is crucial for understanding enzyme mechanisms.
  • Traditional methods like fluorescence spectroscopy have limitations in monitoring fast molecular motions.
  • Carbon nanotube field-effect transistors (CNFETs) offer potential for high-bandwidth electronic detection.

Purpose of the Study:

  • To develop a stable, high-bandwidth transducer for monitoring single protein motion.
  • To investigate the dynamic disorder and processive kinetics of a single lysozyme molecule.
  • To differentiate between single-step and multi-step conformational changes in enzyme activity.

Main Methods:

  • Tethering a single lysozyme molecule to a CNFET.
  • Electronic monitoring of protein motion over extended periods (10 minutes).
  • Statistical analysis of enzymatic hydrolysis and hinge motion rates.

Main Results:

  • Established lysozyme as a processive enzyme, hydrolyzing approximately 100 chemical bonds at 15 Hz before nonproductive hinge motion at 330 Hz.
  • Observed seven independent time scales governing lysozyme activity.
  • Differentiated single-step hinge closure from the two-step enzyme opening process.
  • Determined that pH dependence relates to conformational states, not processive kinetics.

Conclusions:

  • CNFETs provide a powerful tool for studying single-molecule protein dynamics beyond the scope of fluorescence techniques.
  • Lysozyme exhibits complex dynamic behavior, including processive hydrolysis and distinct conformational states.
  • The observed dynamics and pH dependence offer new insights into enzyme mechanism and regulation.