TY  - JOUR
AU  - Li, Jinyu
AU  - Santambrogio, Carlo
AU  - Brocca, Stefania
AU  - Rossetti, Giulia
AU  - Carloni, Paolo
AU  - Grandori, Rita
TI  - Conformational effects in protein electrospray-ionization mass spectrometry
JO  - Mass spectrometry reviews
VL  - 35
IS  - 1
SN  - 0277-7037
CY  - New York, NY [u.a.]
PB  - Wiley
M1  - FZJ-2016-00240
SP  - 111 - 122
PY  - 2016
AB  - 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.
LB  - PUB:(DE-HGF)16
UR  - <Go to ISI:>//WOS:000368739100007
C6  - pmid:25952139
DO  - DOI:10.1002/mas.21465
UR  - https://juser.fz-juelich.de/record/280466
ER  -