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Experimental basis for a new allosteric model for multisubunit proteins.

Cristiano Viappiani1, Stefania Abbruzzetti2, Luca Ronda3

  • 1Departments of Physics and Earth Sciences, NEST, Istituto Nanoscienze, Consiglio Nazionale delle Ricerche, 56127 Pisa, Italy; and cristiano.viappiani@unipr.it eaton@helix.nih.gov.

Proceedings of the National Academy of Sciences of the United States of America
|August 21, 2014
PubMed
Summary

Hemoglobin allostery is explained by a new model where protein structures have two ligand binding phases, not one. Allosteric effectors alter phase fractions, not binding rates, refining the Monod-Wyman-Changeux model.

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Area of Science:

  • Biophysics
  • Biochemistry
  • Structural Biology

Background:

  • The Monod-Wyman-Changeux (MWC) model explains allostery in proteins via equilibrium between reactive (R) and less reactive (T) quaternary structures.
  • In the MWC model, each quaternary structure possesses a single reactivity, influenced by allosteric effectors.

Purpose of the Study:

  • To investigate hemoglobin's allosteric mechanism beyond the traditional MWC model.
  • To explore ligand binding kinetics and quaternary structure dynamics in hemoglobin.

Main Methods:

  • Utilizing silica gels to trap specific protein conformations.
  • Employing novel laser photolysis experiments to probe ligand binding dynamics.

Main Results:

  • Hemoglobin exhibits two distinct ligand binding phases with consistent fast and slow rates in both R and T quaternary structures.
  • Allosteric effectors were found to modulate the proportion of these phases, rather than altering the intrinsic binding rates.

Conclusions:

  • The findings suggest a modification of the MWC model, incorporating a pre-equilibrium between two tertiary conformations within each quaternary structure.
  • This revised model offers insights into the structural basis for differing oxygen affinities between hemoglobin's quaternary states.