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Updated: Jan 7, 2026
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Controlling the Size, Shape and Stability of Supramolecular Polymers in Water
Published on: August 2, 2012
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Protein Confinement Decouples Dynamical Heterogeneity from Structural Preordering in Supercooled Monolayer Water
1State Key Laboratory of Structural Chemistry, Fujian Institute of Research on the Structure of Matter, Chinese Academy of Sciences, Fuzhou, Fujian 350002, China.
JACS Au
|December 26, 2025
Summary
Protein confinement alters supercooled water dynamics, reducing its tendency to form ice. This study reveals how protein interactions change water
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.
Keywords:
dynamical heterogeneityice-like waterprotein-confined waterstructure-dynamic decouplingsupercooled waterMore Related Videos
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