Experiments on Hemoglobin in Single Crystals and Silica Gels Distinguish among Allosteric Models
Trapping quaternary structures of hemoglobin in single crystals or by encapsulation in silica gels has provided a demanding set of data to test statistical mechanical models of allostery. In this work, we compare the results of those experiments with predictions of the four major allosteric models f...
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| Published in | Biophysical journal Vol. 109; no. 6; pp. 1264 - 1272 |
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| Main Authors | , , , , , , , |
| Format | Journal Article |
| Language | English |
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Elsevier Inc
15.09.2015
Biophysical Society The Biophysical Society |
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| Abstract | Trapping quaternary structures of hemoglobin in single crystals or by encapsulation in silica gels has provided a demanding set of data to test statistical mechanical models of allostery. In this work, we compare the results of those experiments with predictions of the four major allosteric models for hemoglobin: the quaternary two-state model of Monod, Wyman, and Changeux; the tertiary two-state model of Henry et al., which is the simplest extension of the Monod-Wyman-Changeux model to include pre-equilibria of tertiary as well as quaternary conformations; the structure-based model of Szabo and Karplus; and the modification of the latter model by Lee and Karplus. We show that only the tertiary two-state model can provide a near quantitative explanation of the single-crystal and gel experimental results. |
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| AbstractList | Trapping quaternary structures of hemoglobin in single crystals or by encapsulation in silica gels has provided a demanding set of data to test statistical mechanical models of allostery. In this work, we compare the results of those experiments with predictions of the four major allosteric models for hemoglobin: the quaternary two-state model of Monod, Wyman, and Changeux; the tertiary two-state model of Henry et al., which is the simplest extension of the Monod-Wyman-Changeux model to include pre-equilibria of tertiary as well as quaternary conformations; the structure-based model of Szabo and Karplus; and the modification of the latter model by Lee and Karplus. We show that only the tertiary two-state model can provide a near quantitative explanation of the single-crystal and gel experimental results. Trapping quaternary structures of hemoglobin in single crystals or by encapsulation in silica gels has provided a demanding set of data to test statistical mechanical models of allostery. In this work, we compare the results of those experiments with predictions of the four major allosteric models for hemoglobin: the quaternary two-state model of Monod, Wyman, and Changeux; the tertiary two-state model of Henry et al., which is the simplest extension of the Monod-Wyman-Changeux model to include pre-equilibria of tertiary as well as quaternary conformations; the structure-based model of Szabo and Karplus; and the modification of the latter model by Lee and Karplus. We show that only the tertiary two-state model can provide a near quantitative explanation of the single-crystal and gel experimental results. |
| Author | Abbruzzetti, Stefania Bettati, Stefano Henry, Eric R. Mozzarelli, Andrea Bruno, Stefano Ronda, Luca Viappiani, Cristiano Eaton, William A. |
| AuthorAffiliation | 4 Department of Physics and Earth Sciences, University of Parma, Parma, Italy 3 Department of Pharmacy, University of Parma, Parma, Italy 6 Department of Life Sciences, University of Parma, Parma, Italy 1 Laboratory of Chemical Physics, NIDDK, National Institutes of Health, Bethesda, Maryland 5 NEST, Nanoscience Institute, CNR, Pisa, Italy 7 Department of Neurosciences, University of Parma, Parma, Italy 2 Institute of Biophysics, CNR, Pisa, Italy |
| AuthorAffiliation_xml | – name: 1 Laboratory of Chemical Physics, NIDDK, National Institutes of Health, Bethesda, Maryland – name: 4 Department of Physics and Earth Sciences, University of Parma, Parma, Italy – name: 7 Department of Neurosciences, University of Parma, Parma, Italy – name: 5 NEST, Nanoscience Institute, CNR, Pisa, Italy – name: 2 Institute of Biophysics, CNR, Pisa, Italy – name: 3 Department of Pharmacy, University of Parma, Parma, Italy – name: 6 Department of Life Sciences, University of Parma, Parma, Italy |
| Author_xml | – sequence: 1 givenname: Eric R. surname: Henry fullname: Henry, Eric R. organization: Laboratory of Chemical Physics, NIDDK, National Institutes of Health, Bethesda, Maryland – sequence: 2 givenname: Andrea surname: Mozzarelli fullname: Mozzarelli, Andrea organization: Institute of Biophysics, CNR, Pisa, Italy – sequence: 3 givenname: Cristiano surname: Viappiani fullname: Viappiani, Cristiano organization: Department of Physics and Earth Sciences, University of Parma, Parma, Italy – sequence: 4 givenname: Stefania surname: Abbruzzetti fullname: Abbruzzetti, Stefania organization: NEST, Nanoscience Institute, CNR, Pisa, Italy – sequence: 5 givenname: Stefano surname: Bettati fullname: Bettati, Stefano organization: Department of Neurosciences, University of Parma, Parma, Italy – sequence: 6 givenname: Luca surname: Ronda fullname: Ronda, Luca organization: Department of Neurosciences, University of Parma, Parma, Italy – sequence: 7 givenname: Stefano surname: Bruno fullname: Bruno, Stefano organization: Institute of Biophysics, CNR, Pisa, Italy – sequence: 8 givenname: William A. surname: Eaton fullname: Eaton, William A. email: eaton@helix.nih.gov organization: Laboratory of Chemical Physics, NIDDK, National Institutes of Health, Bethesda, Maryland |
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| SubjectTerms | Allosteric Regulation Biophysics Experiments Hemoglobin Hemoglobins - chemistry Hemoglobins - metabolism Humans Hydrogen-Ion Concentration Kinetics Models, Molecular Oxygen - chemistry Protein Structure, Quaternary Proteins and Nucleic Acids Silica Silica Gel - chemistry Solutions Temperature |
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| Title | Experiments on Hemoglobin in Single Crystals and Silica Gels Distinguish among Allosteric Models |
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