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Related Concept Videos

Cooperative Allosteric Transitions01:58

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Allosteric Regulation01:08

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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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Bio-layer Interferometry for Measuring Kinetics of Protein-protein Interactions and Allosteric Ligand Effects
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Non-Allosteric Cooperativity in Hemoglobin.

Andrea Bellelli1

  • 1Dipartimento di Scienze Biochimiche "A. Rossi Fanelli", Sapienza University of Rome, Piazzale Aldo Moro 5, 00185 Roma, Italy.

Current Protein & Peptide Science
|November 1, 2017
PubMed
Summary

This study investigates non-allosteric cooperativity in hemoglobin (Hb), proposing it explains puzzling experimental data. Evidence strongly supports effector-induced non-allosteric cooperativity in the T state of hemoglobin.

Keywords:
T state cooperativityTwo-state modelallosteryheterotropic effectorsoxygen bindingthermodynamic linkage.

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Area of Science:

  • Biochemistry
  • Protein Dynamics
  • Molecular Biophysics

Background:

  • Hemoglobin cooperativity is typically explained by allosteric transitions between T and R states.
  • The potential for cooperativity within a single allosteric conformation (non-allosteric cooperativity) has been largely overlooked.

Purpose of the Study:

  • To re-investigate theoretical and experimental evidence for non-allosteric cooperativity in hemoglobin.
  • To explore the role of non-allosteric cooperativity in the T state of hemoglobin, particularly when influenced by effectors.

Main Methods:

  • Theoretical analysis of hemoglobin cooperativity models.
  • Review and synthesis of experimental data related to hemoglobin function.

Main Results:

  • Strong evidence supports effector-induced non-allosteric cooperativity in T state hemoglobin.
  • Non-allosteric cooperativity offers explanations for previously puzzling experimental observations in hemoglobin.

Conclusions:

  • Non-allosteric cooperativity, especially when induced by effectors, is a significant factor in hemoglobin function.
  • This phenomenon helps resolve anomalies in oxygen release, ligand binding, and hybrid hemoglobin behavior.