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Matrix-assisted laser desorption ionization hydrogen/deuterium exchange studies to probe peptide conformational changes

  • Focus: H/D Exchange Of Proteins In Solution
  • Published:
Journal of the American Society for Mass Spectrometry

Abstract

Hydrogen/deuterium (H/D) exchange chemistry monitored by matrix-assisted laser desorption ionization time-of-flight (MALDI-TOF) mass spectrometry is used to study solution phase conformational changes of bradykinin, α-melanocyte stimulating hormone, and melittin as water is added to methanol-d 4, acetonitrile, and isopropanol-d 8 solutions. The results are interpreted in terms of a preference for the peptides to acquire more compact conformations in organic solvents as compared to the random conformations. Our interpretation is supported by circular dichroism spectra of the peptides in the same solvent systems and by previously published structural data for the peptides. These results demonstrate the utility of MALDI-TOF as a method to monitor the H/D exchange chemistry of peptides and investigations of solution-phase conformations of biomolecules.

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  1. Laboratory for Biological Mass Spectrometry, Department of Chemistry, Texas A&M University, P. O. Box 30012, 77842-3012, College Station, TX

    Iddys D. Figueroa & David H. Russell

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  1. Iddys D. Figueroa
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  2. David H. Russell
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Figueroa, I.D., Russell, D.H. Matrix-assisted laser desorption ionization hydrogen/deuterium exchange studies to probe peptide conformational changes. J Am Soc Mass Spectrom 10, 719–731 (1999). https://doi.org/10.1016/S1044-0305(99)00040-9

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  • DOI: https://doi.org/10.1016/S1044-0305(99)00040-9

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