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Related Concept Videos

Primary Active Transport01:29

Primary Active Transport

In contrast to passive transport, active transport involves a substance being moved through membranes in a direction against its concentration or electrochemical gradient. There are two types of active transport: primary active transport and secondary active transport. Primary active transport utilizes chemical energy from ATP to drive protein pumps embedded in the cell membrane. With energy from ATP, the pumps transport ions against their electrochemical gradients—a direction they would not...
Primary Active Transport01:47

Primary Active Transport

In contrast to passive transport, active transport involves a substance being moved through membranes in a direction against its concentration or electrochemical gradient. There are two types of active transport: primary active transport and secondary active transport. Primary active transport utilizes chemical energy from ATP to drive protein pumps that are embedded in the cell membrane. With energy from ATP, the pumps transport ions against their electrochemical gradients—a direction they...
Primary Active Transport01:29

Primary Active Transport

In contrast to passive transport, active transport involves a substance being moved through membranes in a direction against its concentration or electrochemical gradient. There are two types of active transport: primary active transport and secondary active transport. Primary active transport utilizes chemical energy from ATP to drive protein pumps embedded in the cell membrane. With energy from ATP, the pumps transport ions against their electrochemical gradients—a direction they would not...
ATP Driven Pumps II: P-type Pumps01:34

ATP Driven Pumps II: P-type Pumps

The P-type pumps are a large family of integral membrane transporter ATPases. They are divided into five major types based on substrate specificity, from I to V.
A typical P-type pump has three cytosolic domains: nucleotide-binding (N), phosphorylation (P), and activator (A) domains. These domains are connected to the membrane-spanning helices by short amino acid segments. ATP hydrolysis and covalent phosphoenzyme intermediate formation are crucial parts of the catalytic cycle. At the highly...
Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...
Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...

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Related Experiment Video

Updated: Jun 14, 2026

Contribution of the Na+/K+ Pump to Rhythmic Bursting, Explored with Modeling and Dynamic Clamp Analyses
08:34

Contribution of the Na+/K+ Pump to Rhythmic Bursting, Explored with Modeling and Dynamic Clamp Analyses

Published on: May 9, 2021

Allosteric model of an ion pump.

Eiro Muneyuki1, Ken Sekimoto

  • 1Faculty of Science and Engineering, Department of Physics, Chuo University, Kasuga, Bunkyo-ku, Tokyo 112-8551, Japan. emuneyuk@phys.chuo-u.ac.jp

Physical Review. E, Statistical, Nonlinear, and Soft Matter Physics
|April 7, 2010
PubMed
Summary

This study introduces a novel allosteric model for free-energy transduction, demonstrating how coupled subsystems can drive particle transport and regulate function, mimicking biological machinery.

Area of Science:

  • Thermodynamics
  • Biophysics
  • Biochemical Engineering

Background:

  • Biological systems often utilize coupled processes for energy transduction.
  • Understanding the mechanisms of active transport and molecular regulation is crucial.
  • Allosteric coupling is a fundamental principle in protein function.

Purpose of the Study:

  • To develop a simplified model of a free-energy transducer using allosterically coupled ratchet subsystems.
  • To investigate the particle transport dynamics and energy transduction efficiency.
  • To explore the regulatory capabilities and functional similarities to biological systems.

Main Methods:

  • Modeling of two coupled ratchet subsystems.
  • Analysis of correlated transitions in potential profiles.

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Introduction to Solid Supported Membrane Based Electrophysiology
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Introduction to Solid Supported Membrane Based Electrophysiology

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Measuring Cation Transport by Na,K- and H,K-ATPase in Xenopus Oocytes by Atomic Absorption Spectrophotometry: An Alternative to Radioisotope Assays
12:48

Measuring Cation Transport by Na,K- and H,K-ATPase in Xenopus Oocytes by Atomic Absorption Spectrophotometry: An Alternative to Radioisotope Assays

Published on: February 19, 2013

Related Experiment Videos

Last Updated: Jun 14, 2026

Contribution of the Na+/K+ Pump to Rhythmic Bursting, Explored with Modeling and Dynamic Clamp Analyses
08:34

Contribution of the Na+/K+ Pump to Rhythmic Bursting, Explored with Modeling and Dynamic Clamp Analyses

Published on: May 9, 2021

Introduction to Solid Supported Membrane Based Electrophysiology
19:56

Introduction to Solid Supported Membrane Based Electrophysiology

Published on: May 11, 2013

Measuring Cation Transport by Na,K- and H,K-ATPase in Xenopus Oocytes by Atomic Absorption Spectrophotometry: An Alternative to Radioisotope Assays
12:48

Measuring Cation Transport by Na,K- and H,K-ATPase in Xenopus Oocytes by Atomic Absorption Spectrophotometry: An Alternative to Radioisotope Assays

Published on: February 19, 2013

  • Investigation of particle flux ratios and free-energy efficiency.
  • Comparison with the alternate access model for active transport.

    • Main Results:

    • The model demonstrates downhill flux driving uphill flux in coupled subsystems.
    • Flux directionality inverts based on driving flux direction.
    • Variable and nonstoichiometric flux ratios were observed.
    • High efficiencies (up to 90% flux ratio, 40% efficiency) and a stalled state were achieved.
    • The model exhibits regulatory behavior and mimics protein machinery functions.

    Conclusions:

    • Allosteric coupling of subsystems provides a viable mechanism for free-energy transduction.
    • This model offers insights into the origins of diverse protein machinery functions.
    • The model's behavior parallels biological active transport and regulatory systems.