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Related Concept Videos

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...
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...
Allosteric Regulation01:08

Allosteric Regulation

Allosteric regulation of enzymes occurs when the binding of an effector molecule to a site that is different from the active site causes a change in the enzymatic activity. This alternate site is called an allosteric site, and an enzyme can contain more than one of these sites. Allosteric regulation can either be positive or negative, resulting in an increase or decrease in enzyme activity. Most enzymes that display allosteric regulation are metabolic enzymes involved in the degradation or...
Allosteric Regulation01:08

Allosteric Regulation

Allosteric regulation of enzymes occurs when the binding of an effector molecule to a site that is different from the active site causes a change in the enzymatic activity. This alternate site is called an allosteric site, and an enzyme can contain more than one of these sites. Allosteric regulation can either be positive or negative, resulting in an increase or decrease in enzyme activity. Most enzymes that display allosteric regulation are metabolic enzymes involved in the degradation or...
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...

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Updated: Jun 4, 2026

Bio-layer Interferometry for Measuring Kinetics of Protein-protein Interactions and Allosteric Ligand Effects
13:57

Bio-layer Interferometry for Measuring Kinetics of Protein-protein Interactions and Allosteric Ligand Effects

Published on: February 18, 2014

Competing allosteric mechanisms modulate substrate binding in a dimeric enzyme.

Lee A Freiburger1, Oliver M Baettig, Tara Sprules

  • 1Department of Chemistry, McGill University, Montréal, Québec, Canada.

Nature Structural & Molecular Biology
|February 1, 2011
PubMed
Summary
This summary is machine-generated.

Investigating allostery at the molecular level is difficult. This study quantifies allostery using thermodynamics, structure, and dynamics, revealing opposing mechanisms in enzyme-substrate interactions.

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Last Updated: Jun 4, 2026

Bio-layer Interferometry for Measuring Kinetics of Protein-protein Interactions and Allosteric Ligand Effects
13:57

Bio-layer Interferometry for Measuring Kinetics of Protein-protein Interactions and Allosteric Ligand Effects

Published on: February 18, 2014

Comparing the Affinity of GTPase-binding Proteins using Competition Assays
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Published on: October 8, 2015

Unraveling Entropic Rate Acceleration Induced by Solvent Dynamics in Membrane Enzymes
09:42

Unraveling Entropic Rate Acceleration Induced by Solvent Dynamics in Membrane Enzymes

Published on: January 16, 2016

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Structural Biology

Background:

  • Allostery is crucial for biological regulation but challenging to study experimentally.
  • Understanding allosteric mechanisms at a molecular level requires integrated biophysical approaches.

Purpose of the Study:

  • To develop and apply a multi-technique strategy for quantifying allostery.
  • To elucidate the molecular mechanisms governing allosteric regulation in aminoglycoside N-(6')-acetyltransferase-Ii.

Main Methods:

  • Isothermal titration calorimetry (ITC)
  • Circular dichroism (CD) spectroscopy
  • Nuclear magnetic resonance (NMR) spectroscopy

Main Results:

  • Developed a quantitative approach combining ITC, CD, and NMR to analyze allostery.
  • Studied the interaction between aminoglycoside N-(6')-acetyltransferase-Ii and acetyl coenzyme A.
  • Identified opposing allosteric mechanisms: a Koshland-Némethy-Filmer (KNF) paradigm and a ligand-induced partial unfolding mechanism.

Conclusions:

  • Allosteric regulation involves a complex interplay of protein thermodynamics, structure, and dynamics.
  • Ligand binding can be coupled to conformational changes and partial unfolding, modulating allosteric communication.
  • Competition between folding, binding, and conformational changes offers a novel regulatory strategy for enzyme active sites.