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Hall Effect in Dielectric Media: Microwave X-Band Faraday Rotation of Water Adsorbed on Hemoglobin

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Son-Young Chai, Paul O. Vogelhut · 1966

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1966 research used 9.36 GHz microwave Faraday rotation to detect the change from free to bound water on hemoglobin at a hydration level of 0.13 g of water per gram of dry hemoglobin.

Plain English Summary

Summary written for general audiences

This 1966 study used a microwave Faraday rotation technique at 9.36 GHz to examine how water molecules bind to hemoglobin protein. Researchers measured the change from free water to bound water on crystalline bovine hemoglobin powder with variable amounts of adsorbed water, finding that the angle of rotation increased linearly up to a hydration level of about 0.13 g of water per gram of dry hemoglobin and decreased above it.

Why This Matters

This early research used a microwave Faraday rotation technique at 9.36 GHz on crystalline bovine hemoglobin powder to measure the dipole concentration of free water molecules as water adsorbed onto the protein. The angle of rotation increased linearly with adsorbed water until about 0.13 g of water per gram of dry hemoglobin, which the authors define as a critical hydration indicating changes in the structure of bound water. Above that level they discuss the formation of ice-like structures on the hemoglobin surface.

Figures from the Original Paper

Diagrams extracted from the original research document.

diagramPage 4 - AI-described figure: Block diagram of a detecting system for measuring angle rotation.
chartPage 5 - Figure 2: Angle of rotation vs hydration in grams of water per gram hemoglobin.
Cite This Study
Son-Young Chai, Paul O. Vogelhut (1966). Hall Effect in Dielectric Media: Microwave X-Band Faraday Rotation of Water Adsorbed on Hemoglobin.
Show BibTeX
@article{hall_effect_in_dielectric_media_microwave_x_band_faraday_rotation_of_water_adsor_g5607,
  author = {Son-Young Chai and Paul O. Vogelhut},
  title = {Hall Effect in Dielectric Media: Microwave X-Band Faraday Rotation of Water Adsorbed on Hemoglobin},
  year = {1966},
  
  
}
No DOI on file for this study.

Quick Questions About This Study

Researchers used 9.36 GHz microwave radiation to examine how water molecules bind to hemoglobin protein, using a Faraday rotation technique to measure the change from free water to bound water.
Yes, the Faraday rotation technique at 9.36 GHz measured the changes from free water to bound water on hemoglobin. The angle of rotation increased linearly with the amount of adsorbed water up to a hydration level of about 0.13 g of water per gram of dry hemoglobin.
Above 0.13 grams of water per gram of dry hemoglobin, the angle of rotation decreased, and the formation of ice-like structures on the surface of hemoglobin is discussed based on the experimental results. At this level water molecules start to form hydrogen-bonded clusters.
The dipole moments of water molecules in crystalline bovine hemoglobin powder were measured, with variable amounts of adsorbed water.
At X-band frequencies dipoles of water molecules are free to rotate in water structure but no longer free to rotate in ice structure, and microwave techniques eliminate the problems associated with the manufacture of ohmic contacts.