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

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

doi:10.1002/1616-5195(200211)2:8<395::AID-MABI395>3.0.CO;2-9

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

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

Biomedical Engineering

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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 language	English (US)
Pages (from-to)	395-401
Number of pages	7
Journal	Macromolecular Bioscience
Volume	2
Issue number	8
DOIs	https://doi.org/10.1002/1616-5195(200211)2:8<395::AID-MABI395>3.0.CO;2-9
State	Published - Dec 1 2002

Keywords

Coiled-coil
Fusion sequence
Oligomers
Thermal properties

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10.1002/1616-5195(200211)2:8<395::AID-MABI395>3.0.CO;2-9

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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.",

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AU - Wang, Chun

AU - Pechar, Michal

AU - Kopeček, Jindřich

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AB - 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.

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

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Keywords

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