Literature DB >> 11400203

Estimation of proton affinity of proline and tryptophan under electrospray ionization conditions using the extended kinetic method.

S P Mirza1, S Prabhakar, M Vairamani.   

Abstract

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.

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Year:  2001        PMID: 11400203     DOI: 10.1002/rcm.319

Source DB:  PubMed          Journal:  Rapid Commun Mass Spectrom        ISSN: 0951-4198            Impact factor:   2.419


  3 in total

1.  Proton affinity of beta-oxalylaminoalanine (BOAA): incorporation of direct entropy correction into the single-reference kinetic method.

Authors:  Joshua J Wind; Lindsay Papp; Maria Happel; Karen Hahn; Erica J Andriole; John C Poutsma
Journal:  J Am Soc Mass Spectrom       Date:  2005-07       Impact factor: 3.109

2.  The proton affinity of proline analogs using the kinetic method with full entropy analysis.

Authors:  Andrew F Kuntz; Andrew W Boynton; Geoffrey A David; Kathryn E Colyer; John C Poutsma
Journal:  J Am Soc Mass Spectrom       Date:  2002-01       Impact factor: 3.109

3.  Gas-phase reactions of protonated tryptophan.

Authors:  Hadi Lioe; Richard A J O'Hair; Gavin E Reid
Journal:  J Am Soc Mass Spectrom       Date:  2004-01       Impact factor: 3.109

  3 in total

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