FREE SHIPPING over $40
OVER 9000 FIVE-STAR REVIEWS
5% OFF ALL SUBSCRIPTIONS
100% HAPPINESS GUARANTEE
Analyze Diet
0
Home / Equine Research Bank / Biophys J / Electrostatics of hemoglobins from measurements of the elect...
Biophysical journal1995; 68(2); 655-664; doi: 10.1016/S0006-3495(95)80226-2

Electrostatics of hemoglobins from measurements of the electric dichroism and computer simulations.

Abstract: Hemoglobins from normal human cells, from sickle cells, and from horse were investigated by electrooptical methods in their oxy and deoxy forms. The reduced linear dichroism measured as a function of the electric field strength demonstrates the existence of permanent dipole moments in the range of 250-400 Debye units. The reduced limiting dichroism is relatively small (< or = 0.1); it is negative for hemoglobin from sickle cells and positive for the hemoglobins from normal human cells and from horse. The dichroism decay time constants are in the range from about 55 to 90 ns. Calculations of the electrooptical data from available crystal structures are given according to models of various complexity, including Monte Carlo simulations of proton fluctuations with energies evaluated by a finite difference Poisson-Boltzmann procedure. The experimental dipole moments are shown to be consistent with the results of the calculations. In the case of human deoxyhemoglobin, the root mean square dipole is higher than the mean dipole by a factor of about 4.5, indicating a particularly large relative contribution due to proton fluctuations. The ratio of the root mean square dipole to the mean dipole is much smaller (approximately 1.1 to approximately 1.5) for the other hemoglobin molecules. The calculations demonstrate that the dichroism decay time constants are not simply determined by the size/shape of the proteins, but are strongly influenced by the orientation of the dipole vector with respect to the axis of maximal absorbance. The comparison of experimental and calculated electrooptical data provides a useful test for the accuracy of electrostatic calculations and/or for the equivalence of structures in crystals and in solutions.
Get Full Text
Publication Date: 1995-02-01 PubMed ID: 7696517PubMed Central: PMC1281729DOI: 10.1016/S0006-3495(95)80226-2Google Scholar: Lookup
The Equine Research Bank provides access to a large database of publicly available scientific literature. Inclusion in the Research Bank does not imply endorsement of study methods or findings by Mad Barn.
LinkedInCopy
  • Journal Article
  • Research Support
  • U.S. Gov't
  • P.H.S.

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 study explored the electrostatic properties of hemoglobins from normal human cells, sickle cells, and horse cells using electrooptical methods and computer simulations. The results revealed there are permanent dipole moments within the range of 250-400 Debye units in the examined hemoglobins.

Research Methodology

  • The researchers examined hemoglobins from normal human cells, sickle cells, and horse cells. These were analyzed in their oxy and deoxy states.
  • They utilized electrooptical methods to perform this investigation.
  • The electric field strength function was used to gauge the reduced linear dichroism, demonstrating the existence of permanent dipole moments in the given range.
  • The researchers also used crystal structure data to perform calculations of the electrooptical data.
  • These calculations were undertaken using different models of varying complexity, including Monte Carlo simulations with proton fluctuation and energy evaluations with a finite difference Poisson-Boltzmann procedure.

Research Findings

  • The research found that the reduced limiting dichroism, which is relatively small, is negative for hemoglobin from sickle cells but positive for normal human cells and horse cells.
  • It demonstrated that the dichroism decay time constants are in the range of about 55 to 90 ns.
  • The experimental dipole moments were found to be consistent with the results of the calculations.
  • The root mean square dipole of human deoxyhemoglobin is higher than the mean dipole by a factor of about 4.5, signifying a large relative contribution from proton fluctuations.
  • The ratio of the root mean square dipole to the mean dipole is much smaller (approximately 1.1 to approximately 1.5) for other hemoglobin molecules.
  • The calculations indicated that the dichroism decay time constants are influenced strongly by the orientation of the dipole vector relative to the axis of maximal absorbance, rather than simply being determined by the size or shape of the proteins.

Conclusions and Implications

  • The comparison of experimental and calculated electrooptical data provides a useful benchmark for improving the accuracy of electrostatic calculations or testing the equivalence of structures in crystals and in solutions.
  • The study contributes to a greater understanding of the electrostatic properties of different types of hemoglobins, which can have implications in the biomedical field, particularly in the understanding and treatment of related health conditions such as sickle cell disease.

Cite This Article

APA
Antosiewicz J, Porschke D. (1995). Electrostatics of hemoglobins from measurements of the electric dichroism and computer simulations. Biophys J, 68(2), 655-664. https://doi.org/10.1016/S0006-3495(95)80226-2

Publication

Biophysical journal
ISSN: 0006-3495
NlmUniqueID: 0370626
Country: United States
Language: English
Volume: 68
Issue: 2
Pages: 655-664

Researcher Affiliations

Antosiewicz, J
  • Department of Biophysics, Warsaw University, Poland.
Porschke, D

    MeSH Terms

    • Animals
    • Cattle
    • Computer Simulation
    • Electrochemistry
    • Hemoglobin, Sickle / chemistry
    • Hemoglobins / chemistry
    • Horses
    • Humans
    • Hydrogen-Ion Concentration
    • In Vitro Techniques
    • Monte Carlo Method
    • Motion
    • Protein Conformation

    References

    This article includes 33 references
    1. Orttung WH. Calculation of the mean-square dipole moment and proton fluctuation anisotropy of hemoglobin at low ionic strength.. J Phys Chem 1969 Feb;73(2):418-23.
      pubmed: 5773793doi: 10.1021/j100722a026google scholar: lookup
    2. Padlan EA, Love WE. Refined crystal structure of deoxyhemoglobin S. I. Restrained least-squares refinement at 3.0-A resolution.. J Biol Chem 1985 Jul 15;260(14):8272-9.
      pubmed: 4008491doi: 10.2210/pdb1hbs/pdbgoogle scholar: lookup
    3. Bolton W, Perutz MF. Three dimensional fourier synthesis of horse deoxyhaemoglobin at 2.8 Angstrom units resolution.. Nature 1970 Nov 7;228(5271):551-2.
      pubmed: 5472471doi: 10.1038/228551a0google scholar: lookup
    4. Pörschke D. Electric, optical and hydrodynamic parameters of lac repressor from measurements of the electric dichroism. High permanent dipole moment associated with the protein.. Biophys Chem 1987 Nov;28(2):137-47.
      pubmed: 3427205doi: 10.1016/0301-4622(87)80083-2google scholar: lookup
    5. Orttung WH. Anisotropy of proton fluctuations and the Kerr effect of protein solutions. Theoretical considerations.. J Phys Chem 1968 Nov;72(12):4058-66.
      pubmed: 5684770doi: 10.1021/j100858a020google scholar: lookup
    6. Barlow DJ, Thornton JM. The distribution of charged groups in proteins.. Biopolymers 1986 Sep;25(9):1717-33.
      pubmed: 3768483doi: 10.1002/bip.360250913google scholar: lookup
    7. Schlecht P, Vogel H, Mayer A. Effect of oxygen binding on the dielectric properties of hemoglobin.. Biopolymers 1968;6(12):1717-25.
      pubmed: 5704341doi: 10.1002/bip.1968.360061206google scholar: lookup
    8. Schlecht P, Mayer A, Hettner G, Vogel H. Dielectric properties of hemoglobin and myoglobin. I. Influence of solvent and particle size on the dielectric dispersion.. Biopolymers 1969 Jun;7(6):963-74.
      pubmed: 5822432doi: 10.1002/bip.1969.360070611google scholar: lookup
    9. Garcia de la Torre JG, Bloomfield VA. Hydrodynamic properties of complex, rigid, biological macromolecules: theory and applications.. Q Rev Biophys 1981 Feb;14(1):81-139.
      pubmed: 7025081doi: 10.1017/s0033583500002080google scholar: lookup
    10. Orttung WH. Proton binding and dipole moment of hemoglobin. Refined calculations.. Biochemistry 1970 Jun 9;9(12):2394-402.
      pubmed: 5423258doi: 10.1021/bi00814a002google scholar: lookup
    11. Bräunig R, Gushimana Y, Ilgenfritz G. Ionic strength dependence of the electric dissociation field effect. Investigation of 2,6-dinitrophenol and application to the acid-alkaline transition of metmyoglobin and methemoglobin.. Biophys Chem 1987 May 9;26(2-3):181-91.
      pubmed: 3607227doi: 10.1016/0301-4622(87)80021-2google scholar: lookup
    12. Takashima S. Use of protein database for the computation of the dipole moments of normal and abnormal hemoglobins.. Biophys J 1993 May;64(5):1550-8.
      pubmed: 8324190doi: 10.1016/S0006-3495(93)81524-8google scholar: lookup
    13. Antosiewicz J, Porschke D. The nature of protein dipole moments: experimental and calculated permanent dipole of alpha-chymotrypsin.. Biochemistry 1989 Dec 26;28(26):10072-8.
      pubmed: 2620062doi: 10.1021/bi00452a029google scholar: lookup
    14. Warwicker J, Watson HC. Calculation of the electric potential in the active site cleft due to alpha-helix dipoles.. J Mol Biol 1982 Jun 5;157(4):671-9.
      pubmed: 6288964doi: 10.1016/0022-2836(82)90505-8google scholar: lookup
    15. Richards FM. Areas, volumes, packing and protein structure.. Annu Rev Biophys Bioeng 1977;6:151-76.
      pubmed: 326146doi: 10.1146/annurev.bb.06.060177.001055google scholar: lookup
    16. GOEBEL W, VOGEL H. [DIELECTRIC PROPERTIES OF HEMOGLOBIN AND CAUSES OF THEIR GENESIS. I].. Z Naturforsch B 1964 Apr;19:292-302.
      pubmed: 14198187
    17. Porschke D. The mechanism of ion polarisation along DNA double helices.. Biophys Chem 1985 Aug;22(3):237-47.
      pubmed: 4052577doi: 10.1016/0301-4622(85)80046-6google scholar: lookup
    18. Fermi G, Perutz MF, Shaanan B, Fourme R. The crystal structure of human deoxyhaemoglobin at 1.74 A resolution.. J Mol Biol 1984 May 15;175(2):159-74.
      pubmed: 6726807doi: 10.1016/0022-2836(84)90472-8google scholar: lookup
    19. Kirkwood JG, Shumaker JB. The Influence of Dipole Moment Fluctuations on the Dielectric Increment of Proteins in Solution.. Proc Natl Acad Sci U S A 1952 Oct;38(10):855-62.
      pubmed: 16589189doi: 10.1073/pnas.38.10.855google scholar: lookup
    20. Matthew JB, Hanania GI, Gurd FR. Electrostatic effects in hemoglobin: hydrogen ion equilibria in human deoxy- and oxyhemoglobin A.. Biochemistry 1979 May 15;18(10):1919-28.
      pubmed: 435457doi: 10.1021/bi00577a011google scholar: lookup
    21. Porschke D, Meier HJ, Ronnenberg J. Interactions of nucleic acid double helices induced by electric field pulses.. Biophys Chem 1984 Oct;20(3):225-35.
      pubmed: 6498280doi: 10.1016/0301-4622(84)87027-1google scholar: lookup
    22. Hol WG. The role of the alpha-helix dipole in protein function and structure.. Prog Biophys Mol Biol 1985;45(3):149-95.
      pubmed: 3892583doi: 10.1016/0079-6107(85)90001-xgoogle scholar: lookup
    23. Klapper I, Hagstrom R, Fine R, Sharp K, Honig B. Focusing of electric fields in the active site of Cu-Zn superoxide dismutase: effects of ionic strength and amino-acid modification.. Proteins 1986 Sep;1(1):47-59.
      pubmed: 3449851doi: 10.1002/prot.340010109google scholar: lookup
    24. Scheider W. Dielectric Relaxation of Molecules with Fluctuating Dipole Moment.. Biophys J 1965 Sep;5(5):617-28.
      pubmed: 19431340doi: 10.1016/s0006-3495(65)86740-6google scholar: lookup
    25. Porschke D, Jung M. The conformation of single stranded oligonucleotides and of oligonucleotide-oligopeptide complexes from their rotation relaxation in the nanosecond time range.. J Biomol Struct Dyn 1985 Jun;2(6):1173-84.
      pubmed: 3916947doi: 10.1080/07391102.1985.10507631google scholar: lookup
    26. Antosiewicz J, McCammon JA, Gilson MK. Prediction of pH-dependent properties of proteins.. J Mol Biol 1994 May 6;238(3):415-36.
      pubmed: 8176733doi: 10.1006/jmbi.1994.1301google scholar: lookup
    27. Shaanan B. Structure of human oxyhaemoglobin at 2.1 A resolution.. J Mol Biol 1983 Nov 25;171(1):31-59.
      pubmed: 6644819doi: 10.1016/s0022-2836(83)80313-1google scholar: lookup
    28. Teller DC, Swanson E, de Haën C. The translational friction coefficient of proteins.. Methods Enzymol 1979;61:103-24.
      pubmed: 481223doi: 10.1016/0076-6879(79)61010-8google scholar: lookup
    29. Di Iorio EE. Preparation of derivatives of ferrous and ferric hemoglobin.. Methods Enzymol 1981;76:57-72.
      pubmed: 7329277doi: 10.1016/0076-6879(81)76114-7google scholar: lookup
    30. Pörschke D. Structure and dynamics of a tryptophanepeptide-polynucleotide complex.. Nucleic Acids Res 1980 Apr 11;8(7):1591-612.
      pubmed: 6776493doi: 10.1093/nar/8.7.1591google scholar: lookup
    31. Brünger AT, Karplus M. Polar hydrogen positions in proteins: empirical energy placement and neutron diffraction comparison.. Proteins 1988;4(2):148-56.
      pubmed: 3227015doi: 10.1002/prot.340040208google scholar: lookup
    32. Malamud D, Drysdale JW. Isoelectric points of proteins: a table.. Anal Biochem 1978 Jun 1;86(2):620-47.
      pubmed: 26290doi: 10.1016/0003-2697(78)90790-xgoogle scholar: lookup
    33. Eaton WA, Hofrichter J. Polarized absorption and linear dichroism spectroscopy of hemoglobin.. Methods Enzymol 1981;76:175-261.
      pubmed: 7035792doi: 10.1016/0076-6879(81)76126-3google scholar: lookup

    Citations

    This article has been cited 7 times.
    1. Ortega A, Amorós D, García de la Torre J. Prediction of hydrodynamic and other solution properties of rigid proteins from atomic- and residue-level models.. Biophys J 2011 Aug 17;101(4):892-8.
      doi: 10.1016/j.bpj.2011.06.046pubmed: 21843480google scholar: lookup
    2. Kantardjiev AA, Atanasov BP. PHEMTO: protein pH-dependent electric moment tools.. Nucleic Acids Res 2009 Jul;37(Web Server issue):W422-7.
      doi: 10.1093/nar/gkp336pubmed: 19420068google scholar: lookup
    3. Felder CE, Prilusky J, Silman I, Sussman JL. A server and database for dipole moments of proteins.. Nucleic Acids Res 2007 Jul;35(Web Server issue):W512-21.
      doi: 10.1093/nar/gkm307pubmed: 17526523google scholar: lookup
    4. Pan W, Galkin O, Filobelo L, Nagel RL, Vekilov PG. Metastable mesoscopic clusters in solutions of sickle-cell hemoglobin.. Biophys J 2007 Jan 1;92(1):267-77.
      doi: 10.1529/biophysj.106.094854pubmed: 17040989google scholar: lookup
    5. García De La Torre J, Huertas ML, Carrasco B. Calculation of hydrodynamic properties of globular proteins from their atomic-level structure.. Biophys J 2000 Feb;78(2):719-30.
      doi: 10.1016/S0006-3495(00)76630-6pubmed: 10653785google scholar: lookup
    6. Porschke D. Electrostatics and electrodynamics of bacteriorhodopsin.. Biophys J 1996 Dec;71(6):3381-91.
      doi: 10.1016/S0006-3495(96)79531-0pubmed: 8968607google scholar: lookup
    7. Antosiewicz J. Computation of the dipole moments of proteins.. Biophys J 1995 Oct;69(4):1344-54.
      doi: 10.1016/S0006-3495(95)80001-9pubmed: 8534804google scholar: lookup
    Subscribe to our newsletter
    Join 99,344 horse owners like you who receive our email updates on horse health and nutrition.