Abstract
We studied the amino acid frequency and substitution patterns between homologues of prokaryotic species adapted to temperatures in the range 0–102°C, and found a significant temperature-dependent difference in frequency for many of the amino acids. This was particularly clear when we analysed the surface and core residues separately. The difference between the surface and the core is getting more pronounced in proteins adapted to warmer environments, with a more hydrophobic core, and more charged and long-chained amino acids on the surface of the proteins. We also see that mesophiles have a more similar amino acid composition to psychrophiles than to thermophiles, and that archea appears to have a slightly different pattern of substitutions than bacteria.
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Abbreviations
- OGT:
-
Optimal growth temperature
- SASA:
-
Solvent accessible surface area
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Acknowledgements
Thanks to William R. Taylor and Trond H. Bø for valuable input. This research was funded by the Norwegian functional genomics program (FUGE) of the Research Council of Norway, through the Envision project and through the technology platform for bioinformatics.
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Communicated by F. Robb.
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Sælensminde, G., Halskau, Ø., Helland, R. et al. Structure-dependent relationships between growth temperature of prokaryotes and the amino acid frequency in their proteins. Extremophiles 11, 585–596 (2007). https://doi.org/10.1007/s00792-007-0072-3
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DOI: https://doi.org/10.1007/s00792-007-0072-3