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Protein Crowding Effects on Hydration Water Dynamics.

Luigi Caminiti1,2, Maria Taddei1,2, Sara Catalini2,3,4

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This study reveals two distinct structural dynamics in lysozyme hydration water using time-resolved optical Kerr effect spectroscopy. These dynamics are linked to hydrogen bond exchange and protein-induced water reorganization, with a crossover point indicating protein crowding effects.

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Area of Science:

  • Biophysics
  • Physical Chemistry
  • Structural Biology

Background:

  • Understanding water's role in protein structure and function is crucial.
  • Hydration water dynamics are key to protein interactions and stability.
  • Fast time-scale dynamics of water near proteins remain challenging to probe.

Purpose of the Study:

  • To investigate the ultrafast structural and vibrational dynamics of water hydrating lysozyme.
  • To differentiate hydration water dynamics from bulk water and protein contributions.
  • To identify concentration-dependent changes in hydration water behavior.

Main Methods:

  • Time-resolved optical Kerr effect (OKE) spectroscopy.
  • Systematic variation of lysozyme concentration.
  • Analysis of spectral responses to probe structural and vibrational dynamics.

Main Results:

  • Identified two distinct structural dynamics in hydration water: hydrogen bond exchange and protein-induced reorganization.
  • Observed subpicosecond vibrational dynamics of the hydration layer.
  • Detected a crossover point in hydration water properties at a specific protein concentration.

Conclusions:

  • Experimental evidence supports two primary structural dynamics of lysozyme hydration water.
  • The crossover point signifies a transition in water clustering regimes and protein crowding.
  • These findings offer insights into protein-water interactions and the onset of crowding effects.