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Estimation of proton affinity of proline and tryptophan under electrospray ionization conditions using the extended kinetic method
Author(s) -
Mirza Shama P.,
Prabhakar S.,
Vairamani M.
Publication year - 2001
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.319
Subject(s) - chemistry , tryptophan , proline , asparagine , electrospray ionization , valine , amino acid , proton affinity , aspartic acid , glutamic acid , chromatography , mass spectrometry , organic chemistry , biochemistry , ion , protonation
The relative order of the proton affinity (PA) of 20 naturally occurring amino acids has been determined under electrospray ionization conditions and compared with earlier studies of different research workers. The order we obtained is similar to that reported by other groups except in three cases viz., valine–aspartic acid, asparagine–glutamic acid and tryptophan–proline. The PA values of proline and tryptophan are determined by the extended kinetic method using amino acids themselves as reference bases. The PA values we thus obtained for proline and tryptophan are 219.9 and 221.6 kcal/mol, respectively. Copyright © 2001 John Wiley & Sons, Ltd.