SDS-Induced Structural Transitions of Hemoglobin Revealed by Spectroscopic Techniques and Small-Angle Neutron Scattering

Debasish Saha; Mohammad Suhail Khan; Harsh A. Gandhi; Shafinaz Rahman Sarah; Vinod K. Aswal; Jaydeep Bhattacharya

doi:10.1039/d6ma00049e

January 1, 2026Materials AdvancesOpen Access

SDS-Induced Structural Transitions of Hemoglobin Revealed by Spectroscopic Techniques and Small-Angle Neutron Scattering

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Key Points

This research aims to investigate the structural transitions of hemoglobin A₀ upon exposure to sodium dodecyl sulfate (SDS).
Utilized spectroscopic techniques and small-angle neutron scattering to analyze hemoglobin A₀.
Examined the effects of SDS on hemoglobin structure and function through experimental analyses.
Observed significant structural changes in hemoglobin A₀ after SDS treatment, confirming the role of SDS in inducing conformational alterations.

Implication

Reveals structural transitions in hemoglobin induced by SDS, indicating significant biochemical insights.

Abstract

Hemoglobin A₀ (HbA₀) is a physiologically important tetrameric protein, consisting of two alpha (α) and two beta (β) subunits, resides inside the red blood cell and carries oxygen to the...

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Cite This Study

Saha et al. (2026) studied this question.

synapsesocial.com/papers/6a34de1265a5b0777af2d877 https://doi.org/10.1039/d6ma00049e

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SDS-Induced Structural Transitions of Hemoglobin Revealed by Spectroscopic Techniques and Small-Angle Neutron Scattering

Key Points

Implication

Abstract

Discussion

Cite This Study

SDS-Induced Structural Transitions of Hemoglobin Revealed by Spectroscopic Techniques and Small-Angle Neutron Scattering

Key Points

Implication

Abstract

Discussion

Cite This Study

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