ArticleProceedings of the National Academy of Sciences of the United States of America2004
New insights into allosteric mechanisms from trapping unstable protein conformations in silica gels.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.
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Who cites it
37 citing papers in PubMed.
- Analysis of β-C-terminal salt bridges in T-state hemoglobin by trapping tertiary conformations in silica gels.Protein science : a publication of the Protein Society · 2025Article
- Coevolution-Driven Method for Efficiently Simulating Conformational Changes in Proteins Reveals Molecular Details of Ligand Effects in the β2AR Receptor.The journal of physical chemistry. B · 2023Article
- A retrospective on statistical mechanical models for hemoglobin allostery.The Journal of chemical physics · 2022Article
- Structural origin of cooperativity in human hemoglobin: a view from different roles of α and β subunits in the αBiophysical reviews · 2022Review
- Impact of hemoglobin biophysical studies on molecular pathogenesis and drug therapy for sickle cell disease.Molecular aspects of medicine · 2022Review
- Drug discovery by a basic research scientist.Frontiers in molecular biosciences · 2022Article
- Multiple conformations in solution of the maize CHeliyon · 2021Article
- Allosteric control of hemoglobin S fiber formation by oxygen and its relation to the pathophysiology of sickle cell disease.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Immobilization of Allantoinase for the Development of an Optical Biosensor of Oxidative Stress States.Sensors (Basel, Switzerland) · 2019Article
- Tertiary and quaternary structural basis of oxygen affinity in human hemoglobin as revealed by multiscale simulations.Scientific reports · 2017Article
- Experiments on Hemoglobin in Single Crystals and Silica Gels Distinguish among Allosteric Models.Biophysical journal · 2015Article
- From protein structure to function via single crystal optical spectroscopy.Frontiers in molecular biosciences · 2015Review
- In Silico Adoption of an Orphan Nuclear Receptor NR4A1.PloS one · 2015Article
- An Origin of Cooperative Oxygen Binding of Human Adult Hemoglobin: Different Roles of the α and β Subunits in the α2β2 Tetramer.PloS one · 2015Article
- Experimental basis for a new allosteric model for multisubunit proteins.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Differential control of heme reactivity in alpha and beta subunits of hemoglobin: a combined Raman spectroscopic and computational study.Journal of the American Chemical Society · 2014Article
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- Structure of fully liganded Hb ζ2β2s trapped in a tense conformation.Acta crystallographica. Section D, Biological crystallography · 2013Article
- Tertiary and quaternary allostery in tetrameric hemoglobin from Scapharca inaequivalvis.Biochemistry · 2013Article
- Article
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7 authors.
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Abstract
To understand why the classical two-state allosteric model of Monod, Wyman, and Changeux explains cooperative oxygen binding by hemoglobin but does not explain changes in oxygen affinity by allosteric inhibitors, we have investigated the kinetic properties of unstable conformations transiently trapped by encapsulation in silica gels. Conformational trapping reveals that after nanosecond photodissociation of carbon monoxide a large fraction of the subunits of the T quaternary structure has kinetic properties almost identical to those of subunits of the R quaternary structure. Addition of allosteric inhibitors reduces both the fraction of R-like subunits and the oxygen affinity of the T quaternary structure. These kinetic and equilibrium results are readily explained by a recently proposed generalization of the Monod-Wyman-Changeux model in which a pre-equilibrium between two functionally different tertiary, rather than quaternary, conformations plays the central role.
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