Characterizing protein structure in amorphous solids using hydrogen/deuterium exchange with mass spectrometry

Elucidating protein structure in amorphous solids is central to the rational design of stable lyophilized protein drugs. Hydrogen/deuterium (H/D) exchange with electrospray ionization mass spectrometry was applied to lyophilized powders containing calmodulin (17 kDa) and exposed to D 2O vapor at con...

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Veröffentlicht in:	Analytical biochemistry 2007-07, Vol.366 (1), p.18-28
Hauptverfasser:	Li, Yunsong, Williams, Todd D., Schowen, Richard L., Topp, Elizabeth M.
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Amorphous solids Calmodulin - chemistry Calmodulin - genetics Calorimetry, Differential Scanning Chromatography, High Pressure Liquid Deuterium - chemistry Freeze Drying FTIR Hydrogen - chemistry Hydrogen/deuterium exchange Mass spectrometry Molecular Sequence Data Molecular Structure Peptide Fragments - chemistry Peptide Fragments - genetics Powder Diffraction Protein lyophilization Protein structure Protein Structure, Secondary Proteins - chemistry Recombinant Proteins - chemistry Recombinant Proteins - genetics Spectrometry, Mass, Electrospray Ionization Spectroscopy, Fourier Transform Infrared
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