The influence of fusion sequences on the thermal stabilities of coiled-coil proteins

Chunyu Xu, Lisa Joss, Chun Wang, Michal Pechar, Jindřich Kopeček

Research output: Contribution to journalArticlepeer-review

16 Scopus citations

Abstract

Five coiled-coil-containing proteins were synthesized to evaluate the influence of fusion sequences on their thermal stability. All proteins contained the same coiled-coil domain (VSSLESK)6, but differed in the fusion sequence attached. Circular dichroism spectroscopy was used to characterize their secondary structure and thermal stability. The proteins formed a coiled-coil structure, but their melting temperatures were different. The difference in the melting temperatures was not caused by either protein concentration or trace nickel ions. Sedimentation equilibrium experiments suggested an effect of the fusion sequence on the oligomerization state, but did not show a direct relationship between the oligomerization state and the melting temperature.

Original languageEnglish (US)
Pages (from-to)395-401
Number of pages7
JournalMacromolecular Bioscience
Volume2
Issue number8
DOIs
StatePublished - Dec 1 2002

Keywords

  • Coiled-coil
  • Fusion sequence
  • Oligomers
  • Thermal properties

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