Comparision of the Pressure Denaturation of Metmyoglobin in $H_2O$ and $D_2O$

$H_2O$$D_2O$ 에서 메트미오글로빈의 압력에 의한 변성의 비교 연구

  • Keon Kim (Department of Chemistry, Korea University)
  • 김건 (고려대학교 이과대학 화학과)
  • Published : 1984.02.20

Abstract

The stability difference of metmyoglobin in $H_2O$ and $D_2O$ at pH 5.7 and pH 7.0 toward pressure denaturation is studied. Metmyoglobin is denatured in $D_2O$ at smaller pressure than in $H_2O$. The stability difference in $H_2O$ and $D_2O$ is more pronounced at pH 5.7 than at pH 7. The main reasons for the stability difference in $H_2O$ and $D_2O$are the difference in positive charge due to $H^+$and $D^+$ binding to the protein in $H_2O$ and $D_2O$, and the structural change that accompany deuteration.

Keywords

References

  1. Biochim. Biophys. Acta v.36 J. Hermans, Jr;H. A. scheraga
  2. Arch. Biochem. Biophys. v.92 W. F. Harrington;P. H. von Hippel
  3. Biochemistry v.2 D. S. Berns
  4. Biochemistry v.4 P. Appel;L. T. Yang
  5. Biopolymers v.10 P. Appel;W. D. Brown
  6. J. Mol. Biol. v.4 K. Tomita;A, Rich;C. DeLgze;E. R. Blout
  7. Biochemistry v.12 A. P. Zipp;W. Kauzmann
  8. J. Korean Chem. Soc. v.26 I. J. Lee;S. W. Kang;D. S. Shin;K. Kim
  9. J. Amer Chem. Soc. v.73 R. Lumry;E. L. Smith;R. R. Galntz
  10. J. Phys. Chem. v.69 G. C. Krecheck;H. Schneider;H. A. Scheraga
  11. J. Chem. Phys. v.42 A. Ben-Naim
  12. Ph D thesis Princenton University K. Kim
  13. Adv. Protein Chem. v.14 W. Kauzmann
  14. Nature v.177 R. H. Maybury;J. J. Katz