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Effect of buffer cations and of H~3~O^+^ on the charge states of native proteins. Significance to determinations of stability constants of protein complexes by Udo H. Verkerk; Michael Peschke; Paul Kebarle is a Chemistry article available to read on EtoBox.

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## Abstract The progressive reduction of charge in charge states of non‐denatured proteins (lysozyme, ubiquitin, and cytochrome __c__), observed with nanospray in the positive ion mode, when the buffer salt ammonium acetate is replaced by ethylammonium acetates (EtNH~3~Ac, Et~2~NH~2~Ac and Et~3~NHAc) is rationalized on the basis of the charge residue model (CRM). The charge states of the multiply protonated protein are shown to be controlled by the increasing gas‐phase basicities, __GB__(B), of the bases(B) NH~3~, EtNH~2~, Et~2~NH and Et~3~N. Charge states derived from evaluated apparent gas‐phase basicities __GB__^app^ of the basic side‐chains of the protein and the known __GB__(B) of the above bases are found to be in agreement with the experimentally observed charge states. This is a requirement of the CRM, because in this model the small positive ions (the buffer cations in the present case) at the surface of the electrospray droplets are the excess ions that provide the charge of the final small droplet that contains the protein molecule and on evaporation of the solvent transfer the charge to the protein. The observed charge states in the absence of buffer salts, i.e. pure wa

Who reads Effect of buffer cations and of H~3~O^+^ on the charge states of native proteins. Significance to determinations of stability constants of protein complexes?

Author

Udo H. Verkerk; Michael Peschke; Paul Kebarle

Publisher

John Wiley and Sons; Wiley (John Wiley & Sons); Wiley-Blackwell; Wiley-Liss Inc; John Wiley & Sons Inc.; Wiley; Heyden And Son (ISSN 1076-5174)

Published

2003

Language

EN

Field

Chemistry (Physical Sciences)