ArticleLangmuir : the ACS journal of surfaces and colloids2025
Influence of α-Helical Content on the Thermodiffusion of Apomyoglobin.
Article in Langmuir : the ACS journal of surfaces and colloids, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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Who cites it
1 citing paper in PubMed.
- Hydrophilicity controls thermodiffusion in alkylammonium chlorides.The European physical journal. E, Soft matter · 2026Article
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7 authors.
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Abstract
Apo-myoglobin (Apo-Mb) is an extensively studied model system for investigating protein folding due to its distinct stable native, partially folded molten globule (MG), and unfolded states at acidic pH. This study examines the impact of structural conformational changes on the thermodiffusive behavior of Apo-Mb using the infrared thermal diffusion forced Rayleigh scattering (TDFRS) technique. The conformational states were modulated by varying pH and buffer conditions, with their structural changes confirmed via circular dichroism (CD) spectroscopy. The α-helical content decreased with decreasing pH. The thermodiffusion parameter Δ
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