TY  - JOUR
AU  - Li, Jinyu
AU  - Lyu, Wenping
AU  - Rossetti, Giulia
AU  - Konijnenberg, Albert
AU  - Natalello, Antonino
AU  - Ippoliti, Emiliano
AU  - Orozco, Modesto
AU  - Sobott, Frank
AU  - Grandori, Rita
AU  - Carloni, Paolo
TI  - Proton Dynamics in Protein Mass Spectrometry
JO  - The journal of physical chemistry letters
VL  - 8
IS  - 6
SN  - 1948-7185
CY  - Washington, DC
PB  - ACS
M1  - FZJ-2017-03086
SP  - 1105 - 1112
PY  - 2017
AB  - Native electrospray ionization/ion mobility-mass spectrometry (ESI/IM-MS) allows an accurate determination of low-resolution structural features of proteins. Yet, the presence of proton dynamics, observed already by us for DNA in the gas phase, and its impact on protein structural determinants, have not been investigated so far. Here, we address this issue by a multistep simulation strategy on a pharmacologically relevant peptide, the N-terminal residues of amyloid-β peptide (Aβ(1–16)). Our calculations reproduce the experimental maximum charge state from ESI-MS and are also in fair agreement with collision cross section (CCS) data measured here by ESI/IM-MS. Although the main structural features are preserved, subtle conformational changes do take place in the first ∼0.1 ms of dynamics. In addition, intramolecular proton dynamics processes occur on the picosecond-time scale in the gas phase as emerging from quantum mechanics/molecular mechanics (QM/MM) simulations at the B3LYP level of theory. We conclude that proton transfer phenomena do occur frequently during fly time in ESI-MS experiments (typically on the millisecond time scale). However, the structural changes associated with the process do not significantly affect the structural determinants.
LB  - PUB:(DE-HGF)16
UR  - <Go to ISI:>//WOS:000396975600001
C6  - pmid:28207277
DO  - DOI:10.1021/acs.jpclett.7b00127
UR  - https://juser.fz-juelich.de/record/829373
ER  -