Hypothesis on interactions of macromolecules based on molecular vibration patterns in cells and tissues

Front Biosci (Landmark Ed). 2018 Jan 1;23(5):940-946. doi: 10.2741/4626.


The molecular vibration patterns of structure-forming macromolecules in the living cell create very specific electromagnetic frequency patterns which might be used for information on spatial position in the three-dimensional structure as well as the chemical characteristics. Chemical change of a molecule results in a change of the vibration pattern and thus in a change of the emitted electromagnetic frequency pattern. These patterns have to be received by proteins responsible for the necessary interactions and functions. Proteins can function as resonators for frequencies in the range of 1013-1015 Hz. The individual frequency pattern is defined by the amino acid sequence and the polarity of every amino acid caused by their functional groups. If the arriving electromagnetic signal pattern and the emitted pattern of the absorbing protein are matched in relevant parts and in opposite phase, photon energy in the characteristic frequencies can be transferred resulting in a conformational change of that molecule and respectively in an increase of its specific activity. The electromagnetic radiation is very weak. The possibilities to overcome intracellular distances are shown. The motor-driven directed transport of macromolecules starts in the Golgi apparatus. The relevance of molecular interactions based on this signaling for the induction and navigation in the intracellular transport is discussed.

MeSH terms

  • Animals
  • Biophysical Phenomena*
  • Cell Physiological Phenomena*
  • Electromagnetic Fields
  • Golgi Apparatus / metabolism
  • Humans
  • Macromolecular Substances / chemistry*
  • Macromolecular Substances / metabolism*
  • Microtubules / metabolism
  • Models, Theoretical*
  • Molecular Conformation
  • Protein Binding
  • Proteins / chemistry
  • Proteins / metabolism
  • Signal Transduction
  • Vibration


  • Macromolecular Substances
  • Proteins