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Related Concept Videos

Adhesion01:14

Adhesion

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Adhesion occurs when one type of molecule is attracted to a different molecule. Water exhibits adhesive properties in the presence of polar surfaces, such as glass or cellulose in plants. For instance, when water is poured into a glass, the positively charged hydrogen molecules of water are more attracted to the negatively charged oxygen molecules in the silica than to the oxygen in neighboring water molecules.
Capillary action is a result of water’s adhesive tendencies. When a narrow...
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Velocity and Acceleration in Steady and Unsteady Flow01:11

Velocity and Acceleration in Steady and Unsteady Flow

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In fluid mechanics, velocity and acceleration are key concepts for analyzing particle motion in both steady and unsteady flow. Consider a fluid particle moving along a pathline, where its velocity depends on its position and time. The particle's acceleration is obtained by differentiating the velocity with respect to time.
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Accelerators01:17

Accelerators

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Accelerators in concrete serve as admixtures to speed up the hardening process, enabling the concrete to achieve early strength faster. Although accelerators do not necessarily impact the time it takes concrete to set, they reduce this time in practice. A common accelerator is calcium chloride, which is particularly useful for hastening early strength development in cold weather or for rapid repair jobs that require quick heat generation after mixing.
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Turnover Number and Catalytic Efficiency01:19

Turnover Number and Catalytic Efficiency

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The turnover number of an enzyme is the maximum number of substrate molecules it can transform per unit time. Turnover numbers for most enzymes range from 1 to 1000 molecules per second. Catalase has the known highest turnover number, capable of converting up to 2.8×106 molecules of hydrogen peroxide into water and oxygen per second. Lysozyme has the lowest known turnover number of half a molecule per second.
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Catalytically Perfect Enzymes01:07

Catalytically Perfect Enzymes

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The theory of catalytically perfect enzymes was first proposed by W.J. Albery and J. R. Knowles in 1976. These enzymes catalyze biochemical reactions at high-speed. Their catalytic efficiency values range from 108-109 M-1s-1. These enzymes are also called 'diffusion-controlled' as the only rate-limiting step in the catalysis is that of the substrate diffusion into the active site. Examples include triose phosphate isomerase, fumarase, and superoxide dismutase.
 
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Electromotive Force02:36

Electromotive Force

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Electricity is generated by either electrons or ions flowing through a solution or a conducting medium. This flow of electrons or specifically electrical charge is defined as an electric current. When electrons move through a wire, they generate an electric current. It can be recalled  that in a redox reaction, electrons are lost and gained. In the spontaneous redox reaction of zinc  with copper, when zinc is immersed in a copper ion solution, a transfer of electrons from one substance to...
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Related Experiment Video

Updated: Feb 8, 2026

In Vitro and In Vivo Model to Study Bacterial Adhesion to the Vessel Wall Under Flow Conditions
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In Vitro and In Vivo Model to Study Bacterial Adhesion to the Vessel Wall Under Flow Conditions

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Force-activated catalytic pathway accelerates bacterial adhesion against flow.

Jagadish P Hazra1, Nisha Arora1, Amin Sagar1

  • 1Department of Chemical Sciences, Indian Institute of Science Education and Research Mohali, Punjab 140306, India.

The Biochemical Journal
|July 4, 2018
PubMed
Summary
This summary is machine-generated.

Researchers developed a new single-molecule method to track catalytic reaction dynamics in real-time. This revealed a force-induced mechanism that accelerates enzyme activity, offering insights for enzyme design.

Keywords:
bacterial adhesiondynamic force spectroscopyenzyme kineticssingle-molecule intermediate trapping

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Introducing Shear Stress in the Study of Bacterial Adhesion
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Introducing Shear Stress in the Study of Bacterial Adhesion

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Area of Science:

  • Biochemistry and Biophysics
  • Enzyme Catalysis
  • Mechanobiology

Background:

  • Mechanical forces can modulate catalytic reaction pathways and transition states.
  • Real-time tracking of these dynamic changes in enzymatic reactions has been challenging.

Purpose of the Study:

  • To develop a novel method for real-time observation of catalytic reaction dynamics at the single-molecule level.
  • To elucidate the mechano-enzymatic mechanism of sortase A, particularly its role in bacterial adhesion under shear stress.

Main Methods:

  • Single-molecule trapping of reaction intermediates to enable site-specific, real-time reaction monitoring.
  • Nanometer-resolution single-molecule calligraphy.
  • Molecular dynamics simulations incorporating force to analyze enzyme conformational changes.

Main Results:

  • A new method was established to study real-time catalytic pathway dynamics.
  • The sortase A enzymatic reaction was deciphered, showing force-induced enzyme-substrate bond dissociation accelerates the forward reaction 100-fold.
  • Molecular dynamics simulations confirmed a force-induced conformational switch in sortase A, enhancing proton transfer.

Conclusions:

  • A novel mechano-activated catalytic pathway has been identified.
  • This study enables real-time investigation of factors influencing reaction transition states.
  • Findings provide a foundation for the rational design of highly efficient enzymes.