Structure-dependent relationships between growth temperature of prokaryotes and the amino acid frequency in their proteins

Springer Science and Business Media LLC - Tập 11 - Trang 585-596 - 2007
Gisle Sælensminde1,2, Øyvind Halskau3, Ronny Helland4,5, Nils-Peder Willassen5,6, Inge Jonassen1,2
1Computational Biology Unit (CBU), BCCS, University of Bergen, Bergen, Norway
2Department of Informatics, University of Bergen, Bergen, Norway
3Department of Biomedicine, University of Bergen, Bergen, Norway
4Department of Chemistry, University of Tromsø, Tromsø, Norway
5Norwegian Structural Biology Centre, University of Tromsø, Tromsø, Norway
6Institute of Medical Biology, Faculty of Medicine, University of Tromsø, Tromsø, Norway

Tóm tắt

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.

Tài liệu tham khảo

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