Journal Article

FZJ-2015-03435

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png On the Zwitterionic Nature of Gas-Phase Peptides and Protein Ions

Marchese, R. ; Grandori, R. (Corresponding Author) ; Carloni, P.FZJ* ; Raugei, S. (Corresponding Author)

2010
Public Library of Science San Francisco, Calif.

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Please use a persistent id in citations: http://hdl.handle.net/2128/8714  doi:10.1371/journal.pcbi.1000775

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.

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Contributing Institute(s):

1. GRS (GRS)
2. Computational Biomedicine (IAS-5)

Research Program(s):

1. 899 - ohne Topic (POF2-899) (POF2-899)

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Database coverage:
; ; ; ; BIOSIS Previews ; IF < 5 ; JCR ; NCBI Molecular Biology Database ; SCOPUS ; Science Citation Index Expanded ; Thomson Reuters Master Journal List ; Web of Science Core Collection

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