The study of protein conformation in solution via direct sampling by desorption electrospray ionization mass spectrometry

Article

Abstract

The direct sampling feature of liquid sample desorption electrospray ionization (DESI) allows the ionization of liquid samples without adding acids/organic solvents (i.e., without sample pretreatment). As a result, it provides a new approach for probing protein conformation in solution. In this study, it has been observed that native protein ions are generated from proteins in water by DESI. Interestingly, the intensities of the resulting protein ions appear to be higher than those generated by ESI of the proteins in water or in ammonium acetate. For protein solutions that already contain acids/organic solvents, DESI can be used to investigate the influences of these denaturants on protein conformations and the obtained results are in good agreement with spectroscopic data. In addition, online monitoring of protein conformational changes by DESI is feasible; for instance, heat-induced unfolding of ubiquitin can be traced with DESI in water without influences of organic solvents/acids. This DESI method provides a new alternative tool for the study of protein conformation in solution.

Keywords

Protein Conformation Electrospray Ionization Mass Spectrometry TATP Desorption Electrospray Ionization Ambient Mass Spectrometry 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

Supplementary material

13361_2010_211001730_MOESM1_ESM.doc (538 kb)
Supplementary material, approximately 550 KB.

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Copyright information

© American Society for Mass Spectrometry 2010

Authors and Affiliations

  1. 1.Center for Intelligent Chemical Instrumentation, Department of Chemistry and BiochemistryOhio UniversityAthensUSA
  2. 2.Edison Biotechnology Institute, Department of Chemistry and BiochemistryOhio UniversityAthensUSA

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