TITLE

Variation in proton affinity of the guanidino group between free and blocked arginine

AUTHOR(S)
Y. Liu; L. Jin; J.-B. Hou; P.-X. Xu
PUB. DATE
July 2007
SOURCE
Amino Acids;Jul2007, Vol. 33 Issue 1, p145
SOURCE TYPE
Academic Journal
DOC. TYPE
Article
ABSTRACT
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.
ACCESSION #
26015278

 

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