%0 Journal Article
%A Li, Jinyu
%A Santambrogio, Carlo
%A Brocca, Stefania
%A Rossetti, Giulia
%A Carloni, Paolo
%A Grandori, Rita
%T Conformational effects in protein electrospray-ionization mass spectrometry
%J Mass spectrometry reviews
%V 35
%N 1
%@ 0277-7037
%C New York, NY [u.a.]
%I Wiley
%M FZJ-2016-00240
%P 111 - 122
%D 2016
%X Electrospray-ionization mass spectrometry (ESI-MS) is a key tool of structural biology, complementing the information delivered by conventional biochemical and biophysical methods. Yet, the mechanism behind the conformational effects in protein ESI-MS is an object of debate. Two parameters—solvent-accessible surface area (As) and apparent gas-phase basicity (GBapp)—are thought to play a role in controlling the extent of protein ionization during ESI-MS experiments. This review focuses on recent experimental and theoretical investigations concerning the influence of these parameters on ESI-MS results and the structural information that can be derived. The available evidence supports a unified model for the ionization mechanism of folded and unfolded proteins. These data indicate that charge-state distribution (CSD) analysis can provide valuable structural information on normally folded, as well as disordered structures.
%F PUB:(DE-HGF)16
%9 Journal Article
%U <Go to ISI:>//WOS:000368739100007
%$ pmid:25952139
%R 10.1002/mas.21465
%U https://juser.fz-juelich.de/record/280466