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100 | 1 | _ | |a Li, Jinyu |0 P:(DE-Juel1)166112 |b 0 |
245 | _ | _ | |a Conformational effects in protein electrospray-ionization mass spectrometry |
260 | _ | _ | |a New York, NY [u.a.] |c 2016 |b Wiley |
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520 | _ | _ | |a 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. |
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700 | 1 | _ | |a Carloni, Paolo |0 P:(DE-Juel1)145614 |b 4 |u fzj |
700 | 1 | _ | |a Grandori, Rita |0 P:(DE-HGF)0 |b 5 |e Corresponding author |
773 | _ | _ | |a 10.1002/mas.21465 |g Vol. 35, no. 1, p. 111 - 122 |0 PERI:(DE-600)1491946-1 |n 1 |p 111 - 122 |t Mass spectrometry reviews |v 35 |y 2016 |x 0277-7037 |
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