Structural studies of cytochrome P-450 using small angle x-ray scattering.

B. A. Lewis, S. G. Sligar

Research output: Contribution to journalArticlepeer-review

Abstract

We have employed small angle x-ray scattering to examine the solution conformation of cytochrome P-450cam in the presence and absence of its substrate, camphor. The radius of gyration (Rg) of the protein is found to be 23.9 +/- 0.2 A in both states. Comparison of the radius of gyration with that expected for a spherical protein of the same molecular weight indicates that P-450 is an elongated molecule and that its shape may best be approximated by a cylinder about 30 A in diameter and 80 A in length.

Original languageEnglish (US)
Pages (from-to)3599-3601
Number of pages3
JournalJournal of Biological Chemistry
Volume258
Issue number6
StatePublished - Mar 25 1983
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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