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April 10, 2026The Journal of Chemical Physics0 citations

THz spectroscopic fingerprints of the hydration upon globular protein assembly

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LCLuigi CaminitiSNSanjana S. NaligeRTRenato Torre

Key Points

  • The aim is to investigate how hydration dynamics change when globular proteins like lysozyme self-assemble.
  • Utilized THz spectroscopy to examine solvation dynamics at varying protein concentrations.
  • Compared spectral fingerprints with those of liquid-liquid and liquid-solid phase separations.
  • Employed dynamic light scattering to analyze size distribution of lysozyme clusters.
  • Identified distinct THz spectral fingerprints of protein hydration during self-assembly.
  • Demonstrated differences in hydration characteristics between protein assembly and phase separations.
  • Characterization revealed that solvation dynamics provide insights into cluster formation.

Abstract

Lysozyme is a well-known globular protein that can form self-assembled clusters. Here, we report the results of a study on the changes in solvation dynamics upon increasing protein concentration via THz spectroscopy. We find spectral solvation fingerprints in the THz frequency range, which are clearly distinguished from those for liquid-liquid phase separation or liquid-solid phase separation. Furthermore, we carried out supplementary measurements using dynamic light scattering to characterize the size distribution of the protein clusters. This study sheds light on using THz studies of solvation dynamics to characterize and differentiate protein hydration in the case of protein assembly, liquid-liquid phase separation, and liquid-solid phase separation.

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Cite This Study

Caminiti et al. (2026) studied this question.

synapsesocial.com/papers/69d8940c6c1944d70ce050cbhttps://doi.org/10.1063/5.0310494
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