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@ARTICLE{Marchese:201320,
author = {Marchese, Roberto and Grandori, Rita and Carloni, Paolo and
Raugei, Simone},
title = {{A} {C}omputational {M}odel for {P}rotein {I}onization by
{E}lectrospray {B}ased on {G}as-{P}hase {B}asicity},
journal = {Journal of the American Society for Mass Spectrometry},
volume = {23},
number = {11},
issn = {1879-1123},
address = {New York [u.a.]},
publisher = {Springer},
reportid = {FZJ-2015-03625},
pages = {1903 - 1910},
year = {2012},
abstract = {Identifying the key factor(s) governing the overall protein
charge is crucial for the interpretation of
electrospray-ionization mass spectrometry data. Current
hypotheses invoke different principles for folded and
unfolded proteins. Here, first we investigate the gas-phase
structure and energetics of several proteins of variable
size and different folds. The conformer and protomer space
of these proteins ions is explored exhaustively by hybrid
Monte-Carlo/molecular dynamics calculations, allowing for
zwitterionic states. From these calculations, the apparent
gas-phase basicity of desolvated protein ions turns out to
be the unifying trait dictating protein ionization by
electrospray. Next, we develop a simple, general,
adjustable-parameter-free model for the potential energy
function of proteins. The model is capable to predict with
remarkable accuracy the experimental charge of folded
proteins and its well-known correlation with the square root
of protein mass.},
cin = {GRS / IAS-5},
ddc = {530},
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:000309941700008},
doi = {10.1007/s13361-012-0449-0},
url = {https://juser.fz-juelich.de/record/201320},
}