Journal of Protein Chemistry

, Volume 14, Issue 1, pp 27–31

Unfolding of tertiary structure ofHalobacterium halobium flagellins does not result in flagella destruction

Authors

  • V. Yu. Tarasov
    • Institute of Protein ResearchRussian Academy of Sciences
  • A. S. Kostyukova
    • Institute of Protein ResearchRussian Academy of Sciences
  • E. I. Tiktopulo
    • Institute of Protein ResearchRussian Academy of Sciences
  • M. G. Pyatibratov
    • Institute of Protein ResearchRussian Academy of Sciences
  • O. V. Fedorov
    • Institute of Protein ResearchRussian Academy of Sciences
Article

DOI: 10.1007/BF01902841

Cite this article as:
Tarasov, V.Y., Kostyukova, A.S., Tiktopulo, E.I. et al. J Protein Chem (1995) 14: 27. doi:10.1007/BF01902841

Abstract

The structure ofHalobacterium halobium R1M1 flagella is investigated by the methods of scanning microcalorimetry, circular dichroism, and electron microscopy. It is shown that melting curves of flagella in solutions with a different concentration of NaCl display only one peak of heat capacity that corresponds to one cooperatively melting domain. It is found that flagella do not dissociate after melting. The possible structural organization of archaebacterial flagella is discussed.

Key words

Archaebacteriaflagella ofHalobacterium halobiumdomain structureunfolding

Copyright information

© Plenum Publishing Corporation 1995