Energy condensation and dipole alignment in protein dynamics

Area of Science:

• Biophysics
• Computational Biology
• Biochemistry

Background:

• The interaction of distant biomolecules via electromagnetic radiation has been proposed to explain rapid enzymatic reaction rates.
• A theoretical framework suggests proteins need to be in an out-of-equilibrium state, with energy condensed in low-frequency vibrations sustained by hydration layers, for such interactions.

Purpose of the Study:

• To assess the validity of assumptions underpinning the theoretical framework for biomolecular electromagnetic interactions.
• To quantitatively and qualitatively evaluate the role of out-of-equilibrium states and water in protein electromagnetic behavior.

Main Methods:

• Molecular dynamics simulations of bovine serum albumin (BSA) were conducted in four states: equilibrium and out-of-equilibrium in water, and at room and high temperatures in vacuum.
• Physical properties of BSA across these states were compared to evaluate the theoretical model's assumptions.

Main Results:

• Simulations confirmed the theoretical model's assumptions, demonstrating energy condensation at low frequencies and electret-like alignment of protein and water dipoles.
• The out-of-equilibrium state significantly increased the amplitude of BSA's dipole moment oscillations, enhancing potential electromagnetic radiation absorption or emission.
• A quantitative estimate of the contribution of the out-of-equilibrium state and water to the observed phenomena was obtained.

Conclusions:

• The study validates the theoretical framework proposing electromagnetic interactions between distant biomolecules.
• Out-of-equilibrium dynamics and hydration layers are crucial for protein-mediated electromagnetic phenomena.
• The findings provide a method to assess a biomolecule's propensity for electromagnetic interaction with biochemical partners.