Influence of α-Helical Content on the Thermodiffusion of Apomyoglobin.

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 ΔS_T(ΔT), a measure of the temperature sensitivity of the Soret coefficient S_T, also showed a decrease, which is typical

SUBMITTER: Rudani BA 

PROVIDER: S-EPMC12573798 | biostudies-literature | 2025 Oct

REPOSITORIES: biostudies-literature