Correlation between solution and gas-phase protein conformation: H/D exchange, IRMPD, and ESI FT-ICR MS

Michael A. Freitas; Christopher L. Hendrickson; Alan G. Marshall

doi:10.1117/12.380495

22 March 2000 Correlation between solution and gas-phase protein conformation: H/D exchange, IRMPD, and ESI FT-ICR MS

Michael A. Freitas, Christopher L. Hendrickson, Alan G. Marshall

Proceedings Volume 3926, Advances in Nucleic Acid and Protein Analyses, Manipulation, and Sequencing; (2000) https://doi.org/10.1117/12.380495
Event: BiOS 2000 The International Symposium on Biomedical Optics, 2000, San Jose, CA, United States

Abstract

Infrared multiphoton dissociation (IRMPD) of the hydrogen/deuterium (H/D) exchanged 12+ charge state of gas-phase bovine ubiquitin was performed on a Fourier transform ion cyclotron resonance mass spectrometer. The H/D exchange of the 12+ charge state revealed two distinct isotopic distributions indicating the presence of at least two distinct conformations of the 12+ charge state. Following H/D exchange, IRMPD was used to dissociate the conformations. The fragments clearly showed little or no deuterium scrambling as evidenced by a nonstatistical distribution of deuterium incorporation. Analysis of the deuterium incorporation for the five most abundant fragment ions indicated a slow exchanging region of the fast exchanging conformation that corresponds to a stable (beta) - sheet observed by NMR in alcoholic solutions. The data suggest that protection of the amide hydrogens in the (beta) -sheet may result in the observed slow exchange rate and provides further evidence for the retention of secondary structure in gas phase.

Citation Download Citation

Michael A. Freitas, Christopher L. Hendrickson, and Alan G. Marshall "Correlation between solution and gas-phase protein conformation: H/D exchange, IRMPD, and ESI FT-ICR MS", Proc. SPIE 3926, Advances in Nucleic Acid and Protein Analyses, Manipulation, and Sequencing, (22 March 2000); https://doi.org/10.1117/12.380495

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