ArticleProtein science : a publication of the Protein Society2025
Analysis of β-C-terminal salt bridges in T-state hemoglobin by trapping tertiary conformations in silica gels.
Article in Protein science : a publication of the Protein Society, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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2 citing papers in PubMed.
- Quantitative and preliminary clinical assessment of glycohypoxia as an oxygen-unloading defect linking chronic hyperglycemia to low-grade tissue hypoxia in type 2 diabetes: a targeted translational meta-regression with exploratory blood-sample validation.Frontiers in clinical diabetes and healthcare · 2026Article
- 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
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Abstract
Encapsulation of a protein in wet silica gels greatly slows its large-scale motions, allowing the characterization of defined protein conformations during functional and spectroscopic measurements. This technique has revealed the coexistence of two or more functionally distinct tertiary conformations in T-state human hemoglobin, but their structural basis remains unclear. Here, we extend this approach to analyze the β-C-terminal salt bridges in the T-state hemoglobin populations. To this end, we first compare three representative sol-gel trapping protocols by transient absorption characterization of both directions of the hemoglobin allosteric transition (R-to-T and T-to-R) and by O
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