Article
An integrative approach combining ion mobility mass spectrometry, X-ray crystallography, and nuclear magnetic resonance spectroscopy to study the conformational dynamics of α1 -antitrypsin upon ligand binding.
Protein science : a publication of the Protein Society - 1 Aug 2015
Nyon Mun Peak, Prentice Tanya, Day Jemma, Kirkpatrick John, Sivalingam Ganesh N, Levy Geraldine, Haq Imran, Irving James A, Lomas David A, Christodoulou John, Gooptu Bibek, Thalassinos Konstantinos
Abstract excerpt
Native mass spectrometry (MS) methods permit the study of multiple protein species within solution equilibria, whereas ion mobility (IM)-MS can report on conformational behavior of specific states. We used IM-MS to study a conformationally labile protein (α1 -antitrypsin) that undergoes pathological polymerization in the context of point mutations. The folded, native state of the Z-variant remains highly...
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