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Related Concept Videos

Introduction to Mechanisms of Enzyme Catalysis01:13

Introduction to Mechanisms of Enzyme Catalysis

For many years, scientists thought that enzyme-substrate binding took place in a simple "lock-and-key" fashion. This model stated that the enzyme and substrate fit together perfectly in one instantaneous step. However, current research supports a more refined view scientists call induced fit. The induced-fit model expands upon the lock-and-key model by describing a more dynamic interaction between enzyme and substrate. As the enzyme and substrate come together, their interaction causes a mild...
Introduction to Mechanisms of Enzyme Catalysis01:13

Introduction to Mechanisms of Enzyme Catalysis

For many years, scientists thought that enzyme-substrate binding took place in a simple "lock-and-key" fashion. This model stated that the enzyme and substrate fit together perfectly in one instantaneous step. However, current research supports a more refined view scientists call induced fit. The induced-fit model expands upon the lock-and-key model by describing a more dynamic interaction between enzyme and substrate. As the enzyme and substrate come together, their interaction causes a mild...
Enzymes02:34

Enzymes

Inside living organisms, enzymes act as catalysts for many biochemical reactions involved in cellular metabolism. The role of enzymes is to reduce the activation energies of biochemical reactions by forming complexes with its substrates. The lowering of activation energies favor an increase in the rates of biochemical reactions.
Enzyme deficiencies can often translate into life-threatening diseases. For example, a genetic abnormality resulting in the deficiency of the enzyme G6PD...
Induced-fit Model01:13

Induced-fit Model

Most chemical reactions in cells require enzymes—biological catalysts that speed up the reaction without being consumed or permanently changed. They reduce the activation energy needed to convert the reactants into products. Enzymes are proteins, that usually work by binding to a substrate—a reactant molecule that they act upon.
Enzymes exhibit substrate specificity, meaning that they can only bind to certain substrates. This is mainly determined by the shape and chemical characteristics of...
Introduction to Enzyme Kinetics01:19

Introduction to Enzyme Kinetics

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...
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: Jun 14, 2026

Force Spectroscopy of Single Protein Molecules Using an Atomic Force Microscope
06:45

Force Spectroscopy of Single Protein Molecules Using an Atomic Force Microscope

Published on: February 28, 2019

Single-molecule force spectroscopy approach to enzyme catalysis.

Jorge Alegre-Cebollada1, Raul Perez-Jimenez, Pallav Kosuri

  • 1Department of Biological Sciences, Columbia University, New York, New York 10027, USA.

The Journal of Biological Chemistry
|April 13, 2010
PubMed
Summary

Single-molecule force spectroscopy offers a novel way to study enzyme catalysis by applying mechanical force. This technique reveals enzyme dynamics with unprecedented sub-angstrom resolution.

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Last Updated: Jun 14, 2026

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Dissecting Mechanoenzymatic Properties of Processive Myosins with Ultrafast Force-Clamp Spectroscopy
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Area of Science:

  • Biochemistry
  • Biophysics
  • Enzymology

Background:

  • Traditional enzyme catalysis studies rely on bulk biochemistry, X-ray crystallography, and NMR.
  • Single-molecule force spectroscopy (SMFS) using atomic force microscopy (AFM) is an emerging technique.
  • SMFS applies mechanical forces to enzyme substrates, probing catalytic mechanisms.

Purpose of the Study:

  • To introduce SMFS as a powerful tool for enzyme catalysis research.
  • To review current applications and findings of SMFS in enzymology.
  • To discuss the requirements for applying SMFS to new enzyme systems.

Main Methods:

  • Utilizing atomic force microscopy (AFM) to apply piconewton-scale forces.
  • Measuring the force dependence of enzymatic reactions.
  • Analyzing substrate-enzyme interactions at the single-molecule level.

Main Results:

  • SMFS provides sub-angstrom resolution insights into enzyme dynamics.
  • The technique has been successfully applied to study thioredoxin family enzymes.
  • Force-dependent alterations in substrate-enzyme interactions are quantifiable.

Conclusions:

  • SMFS is a revolutionary technique for understanding enzyme catalysis.
  • It offers unique advantages over traditional methods in resolving dynamic processes.
  • Further application of SMFS will expand our knowledge of enzyme mechanisms.