Skip to main content
NCBI 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
. 1975 Jun;72(6):2095–2098. doi: 10.1073/pnas.72.6.2095

Detection of new temperature-dependent conformational transition in lysozyme by carbon-13 nuclear magnetic resonance spectroscopy.

P J Cozzone, S J Opella, O Jardetzky, J Berthou, P Jollès
PMCID: PMC432702  PMID: 1056017

Abstract

A specific temperature-dependent conformational transition of hen egg-white lysozyme, occurring between 20 degree C and 30 degree C in solution, has been detected by 13-C-nuclear magnetic resonance spectroscopy. Selective changes in the chemical shifts of aromatic residues, together with differences in the chemical shifts, and nuclear Overhauser enhancement in the carbonyl, carboxyl, and alpha-carbon regions of the spectrum point to the vicinity of subsites D and E as the primary locus of the structural change.

Full text

PDF
2095

Selected References

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

  1. Allerhand A., Childers R. F., Oldfield E. Carbon-13 Fourier transform NMR studies in 20 mm sample tubes: observation of individual carbon sites in proteins. Ann N Y Acad Sci. 1973 Dec 31;222:764–777. doi: 10.1111/j.1749-6632.1973.tb15303.x. [DOI] [PubMed] [Google Scholar]
  2. Allerhand A., Childers R. F., Oldfield E. Natrual-abundance carbon-13 nuclear magnetic resonance studies in 20-mm sample tubes. Observation of numerous single-carbon resonances of hen egg-white lysozyme. Biochemistry. 1973 Mar 27;12(7):1335–1341. doi: 10.1021/bi00731a013. [DOI] [PubMed] [Google Scholar]
  3. Allerhand A., Cochran D. W., Doddrell D. Carbon-13 Fourier transform nuclear magnetic resonance. II. Ribonuclease. Proc Natl Acad Sci U S A. 1970 Nov;67(3):1093–1096. doi: 10.1073/pnas.67.3.1093. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Berthou J., Jollès P. The influence of urea on crystallization and polymorphism of hen lysozyme. FEBS Lett. 1973 Apr 15;31(2):189–192. doi: 10.1016/0014-5793(73)80100-0. [DOI] [PubMed] [Google Scholar]
  5. Berthou J., Laurent A., Jollès P. Preliminary x-ray investigation of duck egg-white lysozyme II. J Mol Biol. 1972 Nov 28;71(3):815–817. doi: 10.1016/s0022-2836(72)80045-7. [DOI] [PubMed] [Google Scholar]
  6. Blake C. C., Mair G. A., North A. C., Phillips D. C., Sarma V. R. On the conformation of the hen egg-white lysozyme molecule. Proc R Soc Lond B Biol Sci. 1967 Apr 18;167(1009):365–377. doi: 10.1098/rspb.1967.0034. [DOI] [PubMed] [Google Scholar]
  7. Inbar D., Rotman M., Givol D. Crystallization with hapten of the Fab' fragment from a mouse IgA myeloma protein with antidinitrophenyl activity. J Biol Chem. 1971 Oct 25;246(20):6272–6275. [PubMed] [Google Scholar]
  8. Jollès P., Berthou J. High temperature crystallization of lysozyme: an example of phase transition. FEBS Lett. 1972 Jun 1;23(1):21–23. doi: 10.1016/0014-5793(72)80273-4. [DOI] [PubMed] [Google Scholar]
  9. Khechinashvili N. N., Privalov P. L., Tiktopulo E. I. Calorimetric investigation of lysozyme thermal denaturation. FEBS Lett. 1973 Feb 15;30(1):57–60. doi: 10.1016/0014-5793(73)80618-0. [DOI] [PubMed] [Google Scholar]
  10. McDonald C. C., Phillips W. D., Glickson J. D. Nuclear magnetic resonance study of the mechanism of reversible denaturation of lysozyme. J Am Chem Soc. 1971 Jan 13;93(1):235–246. doi: 10.1021/ja00730a039. [DOI] [PubMed] [Google Scholar]
  11. Nakanishi M., Tsuboi M., Ikegami A. Fluctuation of the lysozyme structure. II. Effects of temperature and binding of inhibitors. J Mol Biol. 1973 Apr 25;75(4):673–682. doi: 10.1016/0022-2836(73)90300-8. [DOI] [PubMed] [Google Scholar]
  12. Oesterhelt D., Bauer H., Lynen F. Crystallization of a multienzyme complex: fatty acid synthetase from yeast. Proc Natl Acad Sci U S A. 1969 Aug;63(4):1377–1382. doi: 10.1073/pnas.63.4.1377. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Opella S. J., Nelson D. J., Jardetzyk O. Letter: Carbon magnetic resonance study of the conformational changes in carp muscle calcium binding parvalbumin. J Am Chem Soc. 1974 Oct 30;96(22):7157–7159. doi: 10.1021/ja00829a084. [DOI] [PubMed] [Google Scholar]
  14. SOPHIANOPOULOS A. J., WEISS B. J. THERMODYNAMICS OF CONFORMATIONAL CHANGES OF PROTEINS. I. PH-DEPENDENT DENATURATION OF MURAMIDASE. Biochemistry. 1964 Dec;3:1920–1928. doi: 10.1021/bi00900a023. [DOI] [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