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@ARTICLE{Rudani:1047243,
      author       = {Rudani, Binny A. and Docter, Steffen and Schott-Verdugo,
                      Stephan and Buitenhuis, Johan and Stadler, Andreas M. and
                      Gohlke, Holger and Wiegand, Simone},
      title        = {{I}nfluence of α-{H}elical {C}ontent on the
                      {T}hermodiffusion of {A}pomyoglobin},
      journal      = {Langmuir},
      volume       = {41},
      number       = {42},
      issn         = {0743-7463},
      address      = {Washington, DC},
      publisher    = {ACS Publ.},
      reportid     = {FZJ-2025-04174},
      pages        = {28322–28334},
      year         = {2025},
      note         = {This is an OA article.},
      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
                      ${\color{black}$ 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 $\alpha$-helical content decreased with decreasing pH.
                      The thermodiffusion parameter $\Delta S_{\mathrm{T}}(\Delta
                      T)$, a measure of the temperature sensitivity of the Soret
                      coefficient $S_{\mathrm{T}}$, also showed a decrease, which
                      is typically related to a decreasing hydrophilicity of the
                      solute. Additionally, the buffer composition significantly
                      influenced the thermodiffusive behavior: phosphate buffer
                      promoted Apo-Mb aggregation through electrostatic screening,
                      whereas acetate buffer favored Apo-Mb solubilization.
                      Microsecond-long discrete protonation state constant pH
                      molecular dynamics (CpHMD) simulations support the
                      experimentally observed, pH- and buffer-dependent changes in
                      $\alpha$-helical content and highlight the differences in
                      protein-buffer interactions for phosphate buffer versus
                      acetate buffer. In conclusion, a strong correlation was
                      observed between the thermodiffusion parameter $\Delta
                      S_{\mathrm{T}}(\Delta T)$ and the $\alpha$-helical content,
                      with $\Delta S_{\mathrm{T}}(\Delta T)$ increasing alongside
                      hydrophilicity and $\alpha$-helical content. These findings
                      highlight the role of structural conformation and buffer
                      environment in modulating the thermodiffusive properties of
                      proteins.},
      cin          = {IBG-4 / IBI-4 / JCNS-1},
      ddc          = {540},
      cid          = {I:(DE-Juel1)IBG-4-20200403 / I:(DE-Juel1)IBI-4-20200312 /
                      I:(DE-Juel1)JCNS-1-20110106},
      pnm          = {2172 - Utilization of renewable carbon and energy sources
                      and engineering of ecosystem functions (POF4-217) / 323 -
                      Molecular Targets $\&$ Therapies (POF4-323) / 5241 -
                      Molecular Information Processing in Cellular Systems
                      (POF4-524) / IHRS-BioSoft - International Helmholtz Research
                      School of Biophysics and Soft Matter
                      (IHRS-BioSoft-20061101)},
      pid          = {G:(DE-HGF)POF4-2172 / G:(DE-HGF)POF4-323 /
                      G:(DE-HGF)POF4-5241 / G:(DE-Juel1)IHRS-BioSoft-20061101},
      typ          = {PUB:(DE-HGF)16},
      doi          = {10.1021/acs.langmuir.5c02797},
      url          = {https://juser.fz-juelich.de/record/1047243},
}