Efficient Synthesis ofN-Acyl-α-arylglycines via Palladium-Catalyzed Amidocarbonylation:  Application to the Central Amino Acid of Chloropeptin†

1998 ◽  
Vol 63 (16) ◽  
pp. 5658-5661 ◽  
Author(s):  
Matthias Beller ◽  
Markus Eckert ◽  
E. Wolfgang Holla
Keyword(s):  
Amino Acid ◽  
Efficient Synthesis ◽  
Palladium Catalyzed

scholarly journals Translational Selection and Yeast Proteome Evolution

Genetics ◽  
2003 ◽  
Vol 164 (4) ◽  
pp. 1291-1303 ◽  
Author(s):  
Hiroshi Akashi
Keyword(s):  
Natural Selection ◽  
Amino Acid ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Synonymous Codon ◽  
Amino Acid Usage ◽  
Proper Function ◽  
Efficient Synthesis ◽  
Expression Levels ◽  
Speed And Accuracy

AbstractThe primary structures of peptides may be adapted for efficient synthesis as well as proper function. Here, the Saccharomyces cerevisiae genome sequence, DNA microarray expression data, tRNA gene numbers, and functional categorizations of proteins are employed to determine whether the amino acid composition of peptides reflects natural selection to optimize the speed and accuracy of translation. Strong relationships between synonymous codon usage bias and estimates of transcript abundance suggest that DNA array data serve as adequate predictors of translation rates. Amino acid usage also shows striking relationships with expression levels. Stronger correlations between tRNA concentrations and amino acid abundances among highly expressed proteins than among less abundant proteins support adaptation of both tRNA abundances and amino acid usage to enhance the speed and accuracy of protein synthesis. Natural selection for efficient synthesis appears to also favor shorter proteins as a function of their expression levels. Comparisons restricted to proteins within functional classes are employed to control for differences in amino acid composition and protein size that reflect differences in the functional requirements of proteins expressed at different levels.

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