Comparison of proteins from thermophilic and nonthermophilic sources in terms of structural parameters inferred from amino acid composition.
The amino acid composition of 14 different proteins from thermophilic bacteria were compiled along with the amino acid compositions of 56 corresponding proteins from nonthermophilic sources. A comparison was made between proteins serving the same catalytic function, and significant differences in composition were noted for those proteins from thermophilic bacteria. However, no consistent pattern was evident and the differences were often small. The two data pools were treated as two distinct classes and a thermophilic versus non-thermophilic comparison of amino acid composition was made using the Student's t-test. Significant differences in composition were found for Asx (sum of Asp and Asn, if known), Ser, and Arg. Both classes of data have similar standard deviations for the mean of any single amino acid, suggesting a similar tolerance of variation in the two classes of proteins. This would argue against the hypothesis that thermophiles exhibit a greater frequency of errors in protein synthesis. The amino acid compositions were used to calculate structural parameters (% helix, % beta, % turn, hydrophobicity, and melting temperatures) for the two classes of proteins. Of these, only the predicted % beta content was significantly lower for proteins of thermophilic origin. No differences in hydrophobicity or predicted melting temperature were observed for the two classes of proteins. This study supports the hypothesis that while small differences may occur in the amino acid composition of thermophilic proteins, they are quite varied and often are very subtle.
D000596:Amino Acids / Q000032:analysis*; D000818:Animals; D001419:Bacteria / Q000201:enzymology; D001426:Bacterial Proteins / Q000032:analysis*; D002417:Cattle; D004798:Enzymes / Q000032:analysis; D006801:Humans; D011817:Rabbits; D013552:Swine; D013696:Temperature
D000596:Amino Acids; D001426:Bacterial Proteins; D004798:Enzymes