ArticleJournal of molecular biology2011
WAXS studies of the structural diversity of hemoglobin in solution.
Article in Journal of molecular biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
19 citing papers in PubMed, 30 citations in OpenAlex.
- Dynamic view of an allosteric intermediate in a positively cooperative dimer.bioRxiv : the preprint server for biology · 2026Article
- SAXS/WAXS data of conformationally flexible ribose binding protein.Data in brief · 2024Article
- Biophysical Approaches for the Characterization of Protein-Metabolite Interactions.Methods in molecular biology (Clifton, N.J.) · 2023Review
- Structural origin of cooperativity in human hemoglobin: a view from different roles of α and β subunits in the αBiophysical reviews · 2022Review
- Hemoglobin: Structure, Function and Allostery.Sub-cellular biochemistry · 2020Review
- NMR experiments redefine the hemoglobin binding properties of bacterial NEAr-iron Transporter domains.Protein science : a publication of the Protein Society · 2019Article
- Dynamics of Quaternary Structure Transitions in R-State Carbonmonoxyhemoglobin Unveiled in Time-Resolved X-ray Scattering Patterns Following a Temperature Jump.The journal of physical chemistry. B · 2018Article
- Energetics underlying hemin extraction from human hemoglobin byThe Journal of biological chemistry · 2018Article
- Modulation of hemoglobin dynamics by an allosteric effector.Protein science : a publication of the Protein Society · 2017Article
- Sulfmyoglobin Conformational Change: A Role in the Decrease of Oxy-Myoglobin Functionality.Biochemistry and biophysics reports · 2016Article
- Emerging applications of small angle solution scattering in structural biology.Protein science : a publication of the Protein Society · 2015Review
- New look at hemoglobin allostery.Chemical reviews · 2015Review
- Validating solution ensembles from molecular dynamics simulation by wide-angle X-ray scattering data.Biophysical journal · 2014Article
- The effects of thermal disorder on the solution-scattering profiles of macromolecules.Biophysical journal · 2014Article
- Article
- Comparative analysis of oxy-hemoglobin and aquomet-hemoglobin by hydrogen/deuterium exchange mass spectrometry.Journal of the American Society for Mass Spectrometry · 2013Article
- Probing hemoglobin confinement inside submicron silica tubes using synchrotron SAXS and electrochemical response.European biophysics journal : EBJ · 2013Article
- Wide-angle X-ray solution scattering for protein-ligand binding: multivariate curve resolution with Bayesian confidence intervals.Biophysical journal · 2013Article
- Multi-wavelength anomalous diffraction using medium-angle X-ray solution scattering (MADMAX).Biophysical journal · 2012Article
Corrections and comments
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Authors and funding
10 authors at 4 institutions in 1 country.
Funding
Abstract
Specific ligation states of hemoglobin are, when crystallized, capable of taking on multiple quaternary structures. The relationship between these structures, captured in crystal lattices, and hemoglobin structure in solution remains uncertain. Wide-angle X-ray solution scattering (WAXS) is a sensitive probe of protein structure in solution that can distinguish among similar structures and has the potential to contribute to these issues. We used WAXS to assess the relationships among the structures of human and bovine hemoglobins in different liganded forms in solution. WAXS data readily distinguished among the various forms of hemoglobins. WAXS patterns confirm some of the relationships among hemoglobin structures that have been defined through crystallography and NMR and extend others. For instance, methemoglobin A in solution is, as expected, nearly indistinguishable from HbCO A. Interestingly, for bovine hemoglobin, the differences between deoxy-Hb, methemoglobin and HbCO are smaller than the corresponding differences in human hemoglobin. WAXS data were also used to assess the spatial extent of structural fluctuations of various hemoglobins in solution. Dynamics has been implicated in allosteric control of hemoglobin, and increased dynamics has been associated with lowered oxygen affinity. Consistent with that notion, WAXS patterns indicate that deoxy-Hb A exhibits substantially larger structural fluctuations than HbCO A. Comparisons between the observed WAXS patterns and those predicted on the basis of atomic coordinate sets suggest that the structures of Hb in different liganded forms exhibit clear differences from known crystal structures.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.