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Wongkongkathep P, Li H, Zhang X, et al. Enhancing Protein Disulfide Bond Cleavage by UV Excitation and Electron Capture Dissociation for Top-Down Mass Spectrometry. Int J Mass Spectrom. 2015;390:137-145doi: 10.1016/j.ijms.2015.07.008.
Wongkongkathep, P., Li, H., Zhang, X., Loo, R. R., Julian, R. R., & Loo, J. A. (2015). Enhancing Protein Disulfide Bond Cleavage by UV Excitation and Electron Capture Dissociation for Top-Down Mass Spectrometry. International journal of mass spectrometry, 390137-145. https://doi.org/10.1016/j.ijms.2015.07.008
Wongkongkathep, Piriya, et al. "Enhancing Protein Disulfide Bond Cleavage by UV Excitation and Electron Capture Dissociation for Top-Down Mass Spectrometry." International journal of mass spectrometry vol. 390 (2015): 137-145. doi: https://doi.org/10.1016/j.ijms.2015.07.008
Wongkongkathep P, Li H, Zhang X, Loo RR, Julian RR, Loo JA. Enhancing Protein Disulfide Bond Cleavage by UV Excitation and Electron Capture Dissociation for Top-Down Mass Spectrometry. Int J Mass Spectrom. 2015 Nov 15;390:137-145. doi: 10.1016/j.ijms.2015.07.008. Epub 2015 Jul 23. PMID: 26644781; PMCID: PMC4669582.
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Int J Mass Spectrom. 2015 Nov 15;390:137-145. doi: 10.1016/j.ijms.2015.07.008. Epub 2015 Jul 23.

Enhancing Protein Disulfide Bond Cleavage by UV Excitation and Electron Capture Dissociation for Top-Down Mass Spectrometry.

International journal of mass spectrometry

Piriya Wongkongkathep, Huilin Li, Xing Zhang, Rachel R Ogorzalek Loo, Ryan R Julian, Joseph A Loo

Affiliations

  1. Department of Chemistry and Biochemistry, University of California-Los Angeles Los Angeles, CA 90095.
  2. Department of Biological Chemistry, University of California-Los Angeles Los Angeles, CA 90095.
  3. Department of Chemistry, University of California-Riverside, Riverside, CA 92521.
  4. Department of Chemistry and Biochemistry, University of California-Los Angeles Los Angeles, CA 90095 ; Department of Biological Chemistry, University of California-Los Angeles Los Angeles, CA 90095 ; UCLA/DOE Institute of Genomics and Proteomics, University of California-Los Angeles Los Angeles, CA 90095.

PMID: 26644781 PMCID: PMC4669582 DOI: 10.1016/j.ijms.2015.07.008

Abstract

The application of ion pre-activation with 266 nm ultraviolet (UV) laser irradiation combined with electron capture dissociation (ECD) is demonstrated to enhance top-down mass spectrometry sequence coverage of disulfide bond containing proteins. UV-based activation can homolytically cleave a disulfide bond to yield two separated thiol radicals. Activated ECD experiments of insulin and ribonuclease A containing three and four disulfide bonds, respectively, were performed. UV-activation in combination with ECD allowed the three disulfide bonds of insulin to be cleaved and the overall sequence coverage to be increased. For the larger sized ribonuclease A with four disulfide bonds, irradiation from an infrared laser (10.6 µm) to disrupt non-covalent interactions was combined with UV-activation to facilitate the cleavage of up to three disulfide bonds. Preferences for disulfide bond cleavage are dependent on protein structure and sequence. Disulfide bonds can reform if the generated radicals remain in close proximity. By varying the time delay between the UV-activation and the ECD events, it was determined that disulfide bonds reform within 10-100 msec after their UV-homolytic cleavage.

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