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22 March 2000 Correlation between solution and gas-phase protein conformation: H/D exchange, IRMPD, and ESI FT-ICR MS
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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.
© (2000) COPYRIGHT Society of Photo-Optical Instrumentation Engineers (SPIE). Downloading of the abstract is permitted for personal use only.
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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