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Home / Equine Research Bank / Biophys J / Vibrational modes of hemoglobin in red blood cells.
Biophysical journal1991; 59(2); 363-374; doi: 10.1016/S0006-3495(91)82230-5

Vibrational modes of hemoglobin in red blood cells.

Abstract: Equine red blood cells were washed in saline heavy water (2H2O) to exchange the hydrogen atoms of the non-hemoglobin components with deuterons. This led to novel neutron scattering measurements of protein vibrations within a cellular system and permitted a comparison with inelastic neutron scattering measurements on purified horse hemoglobin, either dry or wetted with 2H2O. As a function of wavevector transfer Q and the frequency transfer v the neutron response typified by the dynamic structure factor S(Q, v) was found to be similar for extracted and cellular hemoglobin at low and high temperatures. At 77 K, in the cells, a peak in S(Q, v) due to the protein was found near 0.7 THz, approximately half the frequency of a strong peak in the aqueous medium. Measurements at higher temperatures (170 and 230 K) indicated similar small shifts downwards in the peak frequencies of both components. At 260 K the low frequency component became predominantly quasielastic, but a significant inelastic component could still be ascribed to the aqueous scattering. Near 295 K the frequency responses of both components were similar and centered near zero. When scattering due to water is taken into account it appears that the protein neutron response in, or out of, red blood cells is little affected by hydration in the low frequency regime where Van der Waals forces are thought to be effective.
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Publication Date: 1991-02-01 PubMed ID: 1849028PubMed Central: PMC1281153DOI: 10.1016/S0006-3495(91)82230-5Google Scholar: Lookup
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Summary

This research summary has been generated with artificial intelligence and may contain errors and omissions. Refer to the original study to confirm details provided. Submit correction.

The research article outlines a study that investigated the vibrational modes of hemoglobin in horse red blood cells, using innovative neutron scattering measurements. The study explored the effects of various factors including temperature and hydration on these vibrational patterns.

Experimental Set-Up and Methodology

  • The study was conducted on equine red blood cells. These cells were washed in saline heavy water (2H2O) for the purpose of replacing the hydrogen atoms within the non-hemoglobin components of the cell with deuterons.
  • This set-up allowed the researchers to achieve groundbreaking neutron scattering measurements of protein vibrations within a living cell system. The results could then be compared with similar measurements taken on purified horse hemoglobin, either dry or saturated with 2H2O.

Measurements and Findings

  • The researchers observed the neutron response typified by the dynamic structure factor S(Q, v) – function of wavevector transfer Q and the frequency transfer v – for both cellular and extracted hemoglobin at varying temperatures.
  • At 77 Kelvin (K), they identified a peak in S(Q, v) correlated to the protein, observed near 0.7 THz, which was about half the frequency of a prominent peak in the aqueous medium.
  • Measurements at higher temperatures (170 and 230 K) showed small downward shifts in peak frequencies for these two components, indicating that temperature significantly impacts these vibrations.

Effect of Hydration

  • At 260 K, the researchers found that the low frequency component had predominantly quasielastic characteristics, although there was still a notable inelastic aspect attributed to the aqueous scattering.
  • Near 295 K, the frequency reactions of these two components were found to be similar, and both were centered near zero.
  • Considering the scattering effect caused by the presence of water, the researchers concluded that the protein’s neutron response, whether inside or outside of red blood cells, was minimally affected by hydration. This observation was particularly true in the low-frequency regime where Van der Waals forces are believed to be effective.

Implications of the Study

  • This study represents a significant breakthrough in biology and biophysics by conducting innovative neutron scattering measurements at a cellular level. It has important implications for the understanding of protein interactions, hydration effects, and cellular behavior at various temperatures.
  • The findings on the minimal effects of hydration can potentially drive further research into protein behavior within cells, and how this affects biological processes at a molecular level.

Cite This Article

APA
Martel P, Calmettes P, Hennion B. (1991). Vibrational modes of hemoglobin in red blood cells. Biophys J, 59(2), 363-374. https://doi.org/10.1016/S0006-3495(91)82230-5

Publication

Biophysical journal
ISSN: 0006-3495
NlmUniqueID: 0370626
Country: United States
Language: English
Volume: 59
Issue: 2
Pages: 363-374

Researcher Affiliations

Martel, P
  • Atomic Energy of Canada Limited, Research Company, Chalk River Nuclear Laboratories, Ontario.
Calmettes, P
    Hennion, B

      MeSH Terms

      • Animals
      • Deuterium
      • Deuterium Oxide
      • Erythrocytes / physiology
      • Hemoglobins / physiology
      • Horses
      • Neutrons
      • Scattering, Radiation
      • Thermodynamics
      • Vibration
      • Water

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      Citations

      This article has been cited 4 times.
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        doi: 10.1007/s00894-008-0446-1pubmed: 19189139google scholar: lookup
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      4. Diehl M, Doster W, Petry W, Schober H. Water-coupled low-frequency modes of myoglobin and lysozyme observed by inelastic neutron scattering.. Biophys J 1997 Nov;73(5):2726-32.
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