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Pairwise Hydrophobicity at Low Temperature: Appearance of a Stable Second Solvent-Separated Minimum with Possible
1Department of Physical Chemistry, Indian Association for the Cultivation of Science , Jadavpur, Kolkata 700032, India.
At low temperatures, a second solvent-separated minimum emerges in hydrophobic interactions, stabilizing ordered water structures. This finding is crucial for understanding cold denaturation in proteins.
Area of Science:
- Physical Chemistry
- Biophysics
- Computational Chemistry
Background:
- The hydrophobic effect is fundamental to protein folding, protein interactions, and membrane assembly.
- Understanding hydrophobic interactions at the molecular level is key to biological processes.
Purpose of the Study:
- To investigate the influence of low temperatures on hydrophobic interactions.
- To analyze the structural changes in water mediating these interactions.
Main Methods:
- Calculated potential of mean force (PMF) using umbrella sampling.
- Simulated interactions between model hydrophobes (methane, cyclobutane, rodlike) at 300 K, 260 K, and 240 K.
Main Results:
- Observed a second solvent-separated minimum (SSSP) in PMF profiles at low temperatures.
- SSSP became more stable than the first solvent-separated pair (FSSP) for cyclobutane and rodlike hydrophobes at 240 K.
- At 240 K, SSSP water for rodlike hydrophobes showed enhanced hydrogen bonding and tetrahedrality.
Conclusions:
- Strongly hydrogen-bonded water structures stabilize the SSSP at low temperatures.
- This stabilization weakens hydrophobic interactions, potentially explaining protein cold denaturation.
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