论文部分内容阅读
The peptide formation of N-phosphoryl aminoacids with amino acids proceeds in aqueous solution withoutany coupling reagents. After being separated in sephadex gelcolumn, the phosphoryl dipeptides were analyzed by theelectrospray ionization tandem mass spectrometry (ESIMS/MS). The result demonstrates that phosphoryl dipeptideswere datected in all the reaction systems. It is found tkat theformation of N-phosphoryl dipeptides is oriented: theN-terminal amino acid residues of the N-phosphoryl dipep-tides are from N-phosphoryl amino acids, and the peptideelongation happened at the C-terminal. Only adipeptide, noβ-dipeptide, is formed in the N-phosphoryl dipeptides,showing that α-carboxylic group is activated selectively byN-pbosphorylation. Theoretical calculation shows that thepeptide formation of N-phosphoryl amino acids might hap-pen through a pentu-coordinate carboxylic-phosphoric in-termediate in solution. These results might give some clues tothe stlidy on the origin of proteins and protein biosynthe
After being separated in sephadex gel column, the phosphoryl dipeptides were analyzed by the electrospray ionization tandem mass spectrometry (ESIMS / MS). The result demonstrates that phosphoryl dipeptideswere datected in all the reaction systems. It is found tkat the formation of N-phosphoryl dipeptides is oriented: the N- terminal amino acid residues of the N-phosphoryl dipep-tides are from N-phosphoryl amino acids, and the peptide establishment occurred at the C-terminal . Only adipeptide, no β-dipeptide, formed in the N-phosphoryl dipeptides, showing that α-carboxylic group is activated selectively by N- pbosphorylation. Theoretical calculation shows that the peptide formation of N-phosphoryl amino acids might hap-pen through a pentu- coordinate carboxylic-phosphoric in-termediate in solution. These results might give some clues tothe stlidy on the origin of proteins and protein biosynthe