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Protein Confinement Decouples Dynamical Heterogeneity from Structural Preordering in Supercooled Monolayer Water.

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Protein confinement alters supercooled water dynamics, reducing its tendency to form ice. This study reveals how protein interactions change water

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Area of Science:

  • Physical chemistry
  • Biophysics
  • Materials science

Background:

  • Supercooled water dynamics under confinement are crucial for biomolecular interactions and cryopreservation.
  • Dynamical heterogeneity in confined water, linked to ice formation, is poorly understood.

Purpose of the Study:

  • Investigate dynamical heterogeneity in protein-confined water monolayers at 240 K.
  • Understand how protein confinement influences water dynamics and ice nucleation.

Main Methods:

  • Isoconfigurational analysis
  • Van Hoff correlation functions
  • Studying protein-confined water monolayers

Main Results:

  • Protein confinement attenuates the local-environment dependence of water's dynamical heterogeneity.
  • The coupling between slow dynamics and ice-like order is diminished under protein confinement, particularly with the PsINP protein.
  • Water at protein interfaces shows no precrystallization slowdown, unlike bulk water.

Conclusions:

  • Protein environments significantly modulate the behavior of deeply supercooled water.
  • Confinement alters water's freezing mechanism, decoupling dynamics from ice-like ordering.
  • Findings offer insights for controlling nanoscale ice formation.