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@ARTICLE{Marchese:201130,
author = {Marchese, Roberto and Grandori, Rita and Carloni, Paolo and
Raugei, Simone},
title = {{O}n the {Z}witterionic {N}ature of {G}as-{P}hase
{P}eptides and {P}rotein {I}ons},
journal = {PLoS Computational Biology},
volume = {6},
number = {5},
issn = {1553-7358},
address = {San Francisco, Calif.},
publisher = {Public Library of Science},
reportid = {FZJ-2015-03435},
pages = {e1000775},
year = {2010},
abstract = {Determining the total number of charged residues
corresponding to a given value of net charge for peptides
and proteins in gas phase is crucial for the interpretation
of mass-spectrometry data, yet it is far from being
understood. Here we show that a novel computational protocol
based on force field and massive density functional
calculations is able to reproduce the experimental facets of
well investigated systems, such as angiotensin II,
bradykinin, and tryptophan-cage. The protocol takes into
account all of the possible protomers compatible with a
given charge state. Our calculations predict that the low
charge states are zwitterions, because the stabilization due
to intramolecular hydrogen bonding and salt-bridges can
compensate for the thermodynamic penalty deriving from
deprotonation of acid residues. In contrast, high charge
states may or may not be zwitterions because internal
solvation might not compensate for the energy cost of charge
separation.},
cin = {GRS / IAS-5},
ddc = {570},
cid = {I:(DE-Juel1)GRS-20100316 / I:(DE-Juel1)IAS-5-20120330},
pnm = {899 - ohne Topic (POF2-899)},
pid = {G:(DE-HGF)POF2-899},
typ = {PUB:(DE-HGF)16},
UT = {WOS:000278759700007},
doi = {10.1371/journal.pcbi.1000775},
url = {https://juser.fz-juelich.de/record/201130},
}