Proteomics

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Mass spectrometric and bio-computational analysis of multiply charged RNase S gas phase complexes obtained by electrospray ionization from varying in-solution equilibrium conditions

ABSTRACT: In this project we investigate the influence of a solvent's composition on the stability of desorbed and multiply charged RNase S ions by analyzing gas phase dissociation reactions triggered by collision induced dissociation (CID) of multiply charged complex ions. RNase S was dissolved in ESI-compatible buffers with either an increasing content of organic co-solvent or with different pH. Direct transition of all ions from the in-solution components is followed by CID of the non-covalent RNase S complex and by quantitative analysis of the dissociation products. From normalized ion abundances are determined the apparent kinetic and apparent thermodynamic gas phase complex properties. The stability of RNase S in the gas phase is independent from the in-solution equilibrium but sensitive to differences in charge states.

INSTRUMENT(S): Waters instrument model

ORGANISM(S): Bos Taurus (bovine)

SUBMITTER: Michael Kreutzer  

LAB HEAD: Prof. Dr. Michael O. Glocker

PROVIDER: PXD027723 | Pride | 2021-11-23

REPOSITORIES: Pride

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Publications

Mass Spectrometric and Bio-Computational Binding Strength Analysis of Multiply Charged RNAse S Gas-Phase Complexes Obtained by Electrospray Ionization from Varying In-Solution Equilibrium Conditions.

Koy Cornelia C   Opuni Kwabena F M KFM   Danquah Bright D BD   Neamtu Andrei A   Glocker Michael O MO  

International journal of molecular sciences 20210922 19

We investigated the influence of a solvent's composition on the stability of desorbed and multiply charged RNAse S ions by analyzing the non-covalent complex's gas-phase dissociation processes. RNAse S was dissolved in electrospray ionization-compatible buffers with either increasing organic co-solvent content or different pHs. The direct transition of all the ions and the evaporation of the solvent from all the in-solution components of RNAse S under the respective in-solution conditions by ele  ...[more]

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