Revising the proton affinity scale of the naturally occurring alpha-amino acids

Christian Bleiholder; Sándor Suhai; Béla Paizs

doi:10.1016/j.jasms.2006.05.010

Revising the proton affinity scale of the naturally occurring alpha-amino acids

J Am Soc Mass Spectrom. 2006 Sep;17(9):1275-81. doi: 10.1016/j.jasms.2006.05.010. Epub 2006 Jul 10.

Authors

Christian Bleiholder¹, Sándor Suhai, Béla Paizs

Affiliation

¹ Department of Molecular Biophysics, German Cancer Research Center, Heidelberg, Germany.

PMID: 16829127
DOI: 10.1016/j.jasms.2006.05.010

Abstract

The proton affinities (PA) of the 20 naturally occurring alpha-amino acids (AA) have been determined computationally by means of density functional theory (DFT) and high-level G2(MP2) calculations. These theoretical PAs, together with data that have appeared since 1997 in the literature, are used to validate the most reasonable currently available PA scale for AAs (Harrison, A. G. Mass Spectrom. Rev. 1997, 16, 201-217.). Significant scatter is observed for the PAs of Ser, Asp, Phe, Asn, Met, Pro, Gln, Glu, Trp, His, Lys, and Arg, many of which have a basic side-chain functionality. Critical review of the available data leads to new consensus PAs for Asn, Gln, Met, and Arg of 222.4, 230.5, 223.7, and 250.2 kcal/mol, respectively.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Algorithms*
Amino Acids / chemistry*
Binding Sites
Computer Simulation
Mass Spectrometry / methods*
Models, Chemical*
Models, Molecular*
Protein Binding
Protons*

Substances

Amino Acids
Protons