Macromolecular bioactivity: is it resonant interaction between macromolecules?--Theory and applications

Area of Science:

• Biophysics
• Molecular Biology
• Biochemistry

Background:

• Biological processes rely on selective biomolecular interactions, primarily driven by proteins.
• The physical mechanisms underlying these crucial protein interactions remain largely unknown.
• Existing models do not fully explain the physical basis of protein-protein and protein-DNA interactions.

Purpose of the Study:

• To propose a novel electromagnetic framework for understanding biomolecular interactions.
• To introduce and detail the Resonant Recognition Model (RRM) for analyzing these interactions.
• To demonstrate the model's ability to predict and design functional biomolecules.

Main Methods:

• Developed the Resonant Recognition Model (RRM) based on electromagnetic principles.
• Investigated periodicities in delocalized electron energy distributions in proteins.
• Introduced protein conductivity to model electromagnetic irradiation and absorption spectra.
• Calculated theoretical spectra in the infrared and visible light ranges.

Main Results:

• Established that specific electron energy periodicities are critical for protein function and target interaction.
• Demonstrated that protein conductivity generates electromagnetic spectra corresponding to energy distributions.
• Validated calculated RRM spectra against experimental data from light-induced biological processes.
• Successfully designed novel peptides with specific spectral characteristics and biological activities.

Conclusions:

• Biomolecular interactions, including protein-protein and protein-DNA binding, are fundamentally electromagnetic.
• The Resonant Recognition Model (RRM) provides a robust theoretical and experimental framework for studying these interactions.
• RRM facilitates the design of new peptides with predictable biological functions based on their electromagnetic properties.