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Proton affinity of arginine measured by the kinetic approach
Author(s) -
Wu Zhuchun,
Fenselau Catherine
Publication year - 1992
Publication title -
rapid communications in mass spectrometry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.528
H-Index - 136
eISSN - 1097-0231
pISSN - 0951-4198
DOI - 10.1002/rcm.1290060610
Subject(s) - chemistry , proton , kinetic energy , arginine , proton affinity , biophysics , biochemistry , nuclear physics , protonation , amino acid , organic chemistry , ion , physics , quantum mechanics , biology
The proton affinity of arginine is obtained from the kinetic method of dissociation of proton‐bound dimers, as 245.2kcal/mol with an uncertainty of ±0.5 kcal/mol higher than that of histidine, the next most basic of the commonly occuring mammalian amino acids, in contrast to the average difference of 1 kcal/mol between the other 19 amino acids. The order of proton affinity of these 20 amino acids is also determined and discussed.