8,700 Studies Reviewed. 87.0% Found Biological Effects. The Evidence is Clear.
Shield Your Body
Whole Body / General

THE MEASUREMENT OF THE COMPLEX DIELECTRIC CONSTANT OF PROTEIN SOLUTIONS AT ULTRA HIGH FREQUENCIES: DIELECTRIC PROPERTIES OF HEMOGLOBIN BOUND WATER

Bioeffects Seen

Bernard E. Pennock · 1968

Share:

1968 research showed microwave frequencies measurably interact with essential blood proteins and their bound water molecules.

Plain English Summary

Summary written for general audiences

This 1968 technical report examined how ultrahigh frequency electromagnetic fields interact with protein solutions, specifically studying hemoglobin and bound water molecules. The research measured dielectric properties (how materials respond to electric fields) at microwave frequencies. This foundational work helped establish how biological molecules behave when exposed to high-frequency electromagnetic energy.

Why This Matters

This early research represents crucial foundational science for understanding how electromagnetic fields interact with biological systems at the molecular level. The study of protein solutions like hemoglobin is particularly significant because proteins are fundamental building blocks of life, and hemoglobin carries oxygen in your blood. What makes this work important is its focus on 'bound water' - the water molecules that attach to proteins and are essential for their function. When microwave frequencies interact with these protein-water complexes, they can alter the dielectric properties that govern how molecules behave electrically. This type of interaction occurs every time you're exposed to microwave radiation from cell phones, WiFi, or other wireless devices. The science demonstrates that biological molecules don't simply ignore electromagnetic fields - they respond in measurable ways that can potentially affect their normal function.

Exposure Information

Specific exposure levels were not quantified in this study.

Cite This Study
Bernard E. Pennock (1968). THE MEASUREMENT OF THE COMPLEX DIELECTRIC CONSTANT OF PROTEIN SOLUTIONS AT ULTRA HIGH FREQUENCIES: DIELECTRIC PROPERTIES OF HEMOGLOBIN BOUND WATER.
Show BibTeX
@article{the_measurement_of_the_complex_dielectric_constant_of_protein_solutions_at_ultra_g6825,
  author = {Bernard E. Pennock},
  title = {THE MEASUREMENT OF THE COMPLEX DIELECTRIC CONSTANT OF PROTEIN SOLUTIONS AT ULTRA HIGH FREQUENCIES: DIELECTRIC PROPERTIES OF HEMOGLOBIN BOUND WATER},
  year = {1968},
  
  
}

Quick Questions About This Study

The research specifically studied hemoglobin, the protein in red blood cells that carries oxygen throughout your body. Hemoglobin was chosen because it's a well-understood protein with clear biological importance for human health and survival.
Bound water molecules are essential for protein function and structure. When electromagnetic fields interact with these protein-water complexes, they can change the electrical properties that govern how proteins work in biological systems.
Dielectric properties describe how biological materials respond to electric fields. These properties determine how electromagnetic energy is absorbed, transmitted, or reflected by proteins and other molecules in living tissue.
Ultrahigh frequencies can alter the electrical characteristics of proteins and their associated water molecules. These changes in dielectric properties can potentially affect how proteins function in normal biological processes.
This foundational work established that biological molecules measurably respond to electromagnetic fields. It provided early scientific evidence that EMF exposure can cause detectable changes in essential proteins like hemoglobin at the molecular level.