caa a22 4500 463186087 CHVBK 20180406164853.0 cr unu---uuuuu 170326e20070701xx s 000 0 eng 10.1007/s00726-006-0401-3 doi (NATIONALLICENCE)springer-10.1007/s00726-006-0401-3 Variation in proton affinity of the guanidino group between free and blocked arginine [Elektronische Daten] [Y. Liu, L. Jin, J.-B. Hou, P.-X. Xu, Y.-F. Zhao] Summary.: In this paper, the analog of arginine residues in peptides was synthesized and characterized by ESI-MS/MS (electrospray ionization with tandem mass spectrometry), 31P NMR, 1H NMR, IR and high-resolution mass spectrometry. When the Todd reaction activity of the guanidino group in free arginine and the arginine peptide analog were compared, it was found that the proton affinity of the guanidino group was decreased when both the N- and the C-terminal were blocked. As a result, the guanidino group of arginine residues in peptides could be phosphorylated under the Todd reaction condition, but not the free arginine. This result was further proved by the theoretical calculation of their proton affinity. Springer-Verlag, 2006 Keywords: Arginine residues - Guanidino group - Proton affinity - Todd reaction nationallicence Liu Y. The Key Laboratory for Chemical Biology of Fujian Province, Department of Chemistry, College of Chemistry and Chemical Engineering, Xiamen University, Xiamen, China aut Jin L. The Key Laboratory for Chemical Biology of Fujian Province, Department of Chemistry, College of Chemistry and Chemical Engineering, Xiamen University, Xiamen, China aut Hou J.-B The Key Laboratory for Chemical Biology of Fujian Province, Department of Chemistry, College of Chemistry and Chemical Engineering, Xiamen University, Xiamen, China aut Xu P.-X The Key Laboratory for Chemical Biology of Fujian Province, Department of Chemistry, College of Chemistry and Chemical Engineering, Xiamen University, Xiamen, China aut Zhao Y.-F The Key Laboratory for Chemical Biology of Fujian Province, Department of Chemistry, College of Chemistry and Chemical Engineering, Xiamen University, Xiamen, China aut Amino Acids Springer-Verlag 33/1(2007-07-01), 145-150 0939-4451 33:1<145 2007 33 726 https://doi.org/10.1007/s00726-006-0401-3 text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1007/s00726-006-0401-3 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Liu Y. The Key Laboratory for Chemical Biology of Fujian Province, Department of Chemistry, College of Chemistry and Chemical Engineering, Xiamen University, Xiamen, China aut NATIONALLICENCE 700 1- Jin L. The Key Laboratory for Chemical Biology of Fujian Province, Department of Chemistry, College of Chemistry and Chemical Engineering, Xiamen University, Xiamen, China aut NATIONALLICENCE 700 1- Hou J.-B The Key Laboratory for Chemical Biology of Fujian Province, Department of Chemistry, College of Chemistry and Chemical Engineering, Xiamen University, Xiamen, China aut NATIONALLICENCE 700 1- Xu P.-X The Key Laboratory for Chemical Biology of Fujian Province, Department of Chemistry, College of Chemistry and Chemical Engineering, Xiamen University, Xiamen, China aut NATIONALLICENCE 700 1- Zhao Y.-F The Key Laboratory for Chemical Biology of Fujian Province, Department of Chemistry, College of Chemistry and Chemical Engineering, Xiamen University, Xiamen, China aut NATIONALLICENCE 773 0- Amino Acids Springer-Verlag 33/1(2007-07-01), 145-150 0939-4451 33:1<145 2007 33 726 Metadata rights reserved Springer special CC-BY-NC licence nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-springer