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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...
Alterations in Muscle Tone lll01:11

Alterations in Muscle Tone lll

Rigidity and myotonia are distinct abnormalities of muscle tone that affect resistance and relaxation during movement. Although both involve altered muscle contraction, they arise from different neurological and muscular mechanisms.CharacteristicsRigidity is characterized by uniform resistance to passive movement across the entire range, independent of speed, affecting flexors and extensors equally. It may appear as lead-pipe rigidity (smooth, constant resistance) or cogwheel rigidity...
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...

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Related Experiment Video

Updated: Jun 6, 2026

Flexural Rigidity Measurements of Biopolymers Using Gliding Assays
07:55

Flexural Rigidity Measurements of Biopolymers Using Gliding Assays

Published on: November 9, 2012

Correlating allostery with rigidity.

A J Rader1, Stephen M Brown

  • 1Department of Physics, Indiana University-Purdue University Indianapolis, Indianapolis, IN 46202, USA. ajrader@iupui.edu

Molecular Biosystems
|November 10, 2010
PubMed
Summary
This summary is machine-generated.

Allosteric proteins regulate cellular processes by changing shape. Rigidity analysis reveals a rigid path connecting effector and catalytic sites, explaining how distant sites communicate in allosteric regulation.

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Biophysics

Background:

  • Allostery is a key biological regulatory mechanism involving ligand binding at one site affecting another.
  • Allosteric regulation often involves communication between distant catalytic and effector sites.
  • Understanding the structural basis of allosteric communication is crucial for deciphering cellular processes.

Purpose of the Study:

  • To investigate the role of structural rigidity in allosteric regulation.
  • To test the hypothesis that catalytic and effector sites are structurally coupled in allosteric proteins.
  • To explore novel methods for analyzing allosteric mechanisms.

Main Methods:

  • Rigidity analysis using graph theory on protein structures.
  • Comparison of protein structures in inactive (T) and active (R) states.
  • Identification of rigid pathways connecting effector and catalytic sites.

Main Results:

  • Allosteric transitions show a global change in rigidity, with the R state being more rigid than the T state.
  • A rigid path connecting effector and catalytic sites was observed in 68.75% of the studied allosteric proteins.
  • Structural rigidity appears to be a fundamental property underlying allosteric communication.

Conclusions:

  • Protein structural rigidity plays a fundamental role in allosteric regulation.
  • Rigid pathways facilitate communication between distal effector and catalytic sites.
  • This study provides new insights into the physical mechanisms governing allostery.