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. CD spectrum of the coiled-coil-containing proteins (10 × 10−6 M) in 10 × 10−3 M PBS buffer at 25 °C.
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