Skip to main content
PMC home page
Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1985 Aug;82(15):5000–5004. doi: 10.1073/pnas.82.15.5000

Protein states and proteinquakes.

A Ansari, J Berendzen, S F Bowne, H Frauenfelder, I E Iben, T B Sauke, E Shyamsunder, R D Young
PMCID: PMC390486  PMID: 3860839

Abstract

After photodissociation of carbon monoxide bound to myoglobin, the protein relaxes to the deoxy equilibrium structure in a quake-like motion. Investigation of the proteinquake and of related intramolecular equilibrium motions shows that states and motions have a hierarchical glass-like structure.

Full text

PDF
5000

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Austin R. H., Beeson K. W., Eisenstein L., Frauenfelder H., Gunsalus I. C. Dynamics of ligand binding to myoglobin. Biochemistry. 1975 Dec 2;14(24):5355–5373. doi: 10.1021/bi00695a021. [DOI] [PubMed] [Google Scholar]
  2. Bauminger E. R., Cohen S. G., Nowik I., Ofer S., Yariv J. Dynamics of heme iron in crystals of metmyoglobin and deoxymyoglobin. Proc Natl Acad Sci U S A. 1983 Feb;80(3):736–740. doi: 10.1073/pnas.80.3.736. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Bennett W. S., Huber R. Structural and functional aspects of domain motions in proteins. CRC Crit Rev Biochem. 1984;15(4):291–384. doi: 10.3109/10409238409117796. [DOI] [PubMed] [Google Scholar]
  4. Blumenfeld L. A. The physical aspects of energy transduction in biological systems. Q Rev Biophys. 1978 Aug;11(3):251–308. doi: 10.1017/s0033583500002286. [DOI] [PubMed] [Google Scholar]
  5. Cooper A. Thermodynamic fluctuations in protein molecules. Proc Natl Acad Sci U S A. 1976 Aug;73(8):2740–2741. doi: 10.1073/pnas.73.8.2740. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Eaton W. A., Hofrichter J. Polarized absorption and linear dichroism spectroscopy of hemoglobin. Methods Enzymol. 1981;76:175–261. doi: 10.1016/0076-6879(81)76126-3. [DOI] [PubMed] [Google Scholar]
  7. Eftink M. R., Ghiron C. A. Dynamics of a protein matrix revealed by fluorescence quenching. Proc Natl Acad Sci U S A. 1975 Sep;72(9):3290–3294. doi: 10.1073/pnas.72.9.3290. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Frauenfelder H., Petsko G. A., Tsernoglou D. Temperature-dependent X-ray diffraction as a probe of protein structural dynamics. Nature. 1979 Aug 16;280(5723):558–563. doi: 10.1038/280558a0. [DOI] [PubMed] [Google Scholar]
  9. Friedman J. M., Scott T. W., Stepnoski R. A., Ikeda-Saito M., Yonetani T. The iron-proximal histidine linkage and protein control of oxygen binding in hemoglobin. A transient Raman study. J Biol Chem. 1983 Sep 10;258(17):10564–10572. [PubMed] [Google Scholar]
  10. Gelin B. R., Lee A. W., Karplus M. Hemoglobin tertiary structural change on ligand binding. Its role in the co-operative mechanism. J Mol Biol. 1983 Dec 25;171(4):489–559. doi: 10.1016/0022-2836(83)90042-6. [DOI] [PubMed] [Google Scholar]
  11. Genzel L., Kremer F., Poglitsch A., Bechtold G. Relaxation process on a picosecond time scale in hemoglobin and poly(L-alanine) observed by millimeter-wave spectroscopy. Biopolymers. 1983 Jul;22(7):1715–1729. doi: 10.1002/bip.360220708. [DOI] [PubMed] [Google Scholar]
  12. Henry E. R., Levitt M., Eaton W. A. Molecular dynamics simulation of photodissociation of carbon monoxide from hemoglobin. Proc Natl Acad Sci U S A. 1985 Apr;82(7):2034–2038. doi: 10.1073/pnas.82.7.2034. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Iizuka T., Yamamoto H., Kotani M., Yonetani T. Low temperature photodissociation of hemoproteins: carbon monoxide complex of myoglobin and hemoglobin. Biochim Biophys Acta. 1974 Nov 5;371(1):126–139. doi: 10.1016/0005-2795(74)90161-5. [DOI] [PubMed] [Google Scholar]
  14. Janin J., Wodak S. J. Structural domains in proteins and their role in the dynamics of protein function. Prog Biophys Mol Biol. 1983;42(1):21–78. doi: 10.1016/0079-6107(83)90003-2. [DOI] [PubMed] [Google Scholar]
  15. Krupyanskii YuF, Parak F., Goldanskii V. I., Mössbauer R. L., Gaubman E. E., Engelmann H., Suzdalev I. P. Investigation of large intramolecular movement within metmyoglobin by Rayleigh scattering of Mössbauer radiation (RSMR). Z Naturforsch C. 1982 Jan-Feb;37(1-2):57–62. doi: 10.1515/znc-1982-1-211. [DOI] [PubMed] [Google Scholar]
  16. Lakowicz J. R., Weber G. Quenching of protein fluorescence by oxygen. Detection of structural fluctuations in proteins on the nanosecond time scale. Biochemistry. 1973 Oct 9;12(21):4171–4179. doi: 10.1021/bi00745a021. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Martin J. L., Migus A., Poyart C., Lecarpentier Y., Astier R., Antonetti A. Femtosecond photolysis of CO-ligated protoheme and hemoproteins: appearance of deoxy species with a 350-fsec time constant. Proc Natl Acad Sci U S A. 1983 Jan;80(1):173–177. doi: 10.1073/pnas.80.1.173. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Ondrias M. R., Rousseau D. L., Simon S. R. Resonance Raman spectra of photodissociated carbonmonoxy hemoglobin and deoxy hemoglobin at 10 K. J Biol Chem. 1983 May 10;258(9):5638–5642. [PubMed] [Google Scholar]
  19. Parak F., Frolov E. N., Mössbauer R. L., Goldanskii V. I. Dynamics of metmyoglobin crystals investigated by nuclear gamma resonance absorption. J Mol Biol. 1981 Feb 5;145(4):825–833. doi: 10.1016/0022-2836(81)90317-x. [DOI] [PubMed] [Google Scholar]
  20. Parak F., Knapp E. W. A consistent picture of protein dynamics. Proc Natl Acad Sci U S A. 1984 Nov;81(22):7088–7092. doi: 10.1073/pnas.81.22.7088. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Phillips S. E. Structure and refinement of oxymyoglobin at 1.6 A resolution. J Mol Biol. 1980 Oct 5;142(4):531–554. doi: 10.1016/0022-2836(80)90262-4. [DOI] [PubMed] [Google Scholar]
  22. Roder H., Berendzen J., Bowne S. F., Frauenfelder H., Sauke T. B., Shyamsunder E., Weissman M. B. Comparison of the magnetic properties of deoxy- and photodissociated myoglobin. Proc Natl Acad Sci U S A. 1984 Apr;81(8):2359–2363. doi: 10.1073/pnas.81.8.2359. [DOI] [PMC free article] [PubMed] [Google Scholar]
  23. Sharonov Y. A., Sharonova N. A., Figlovsky V. A., Grigorjev V. A. A comparison of the heme electronic states in equilibrium and nonequilibrium protein conformations of high-spin ferrous hemoproteins. Low temperature magnetic circular dichroism studies. Biochim Biophys Acta. 1982 Dec 20;709(2):332–341. doi: 10.1016/0167-4838(82)90476-9. [DOI] [PubMed] [Google Scholar]
  24. Spartalian K., Lang G., Yonetani T. Low temperature photodissociation studies of ferrous hemoglobin and myoglobin complexes by Mössbauer spectroscopy. Biochim Biophys Acta. 1976 Apr 23;428(2):281–290. doi: 10.1016/0304-4165(76)90036-2. [DOI] [PubMed] [Google Scholar]
  25. Stein D. L. A model of protein conformational substates. Proc Natl Acad Sci U S A. 1985 Jun;82(11):3670–3672. doi: 10.1073/pnas.82.11.3670. [DOI] [PMC free article] [PubMed] [Google Scholar]

Articles from Proceedings of the National Academy of Sciences of the United States of America are provided here courtesy of National Academy of Sciences

RESOURCES