An integrative approach combining ion mobility mass spectrometry, X-ray crystallography, and nuclear magnetic resonance spectroscopy to study the conformational dynamics of α(1)-antitrypsin upon ligand binding

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 (α(1)-antitrypsin) that undergoes pathologica...

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Detalles Bibliográficos
Autores principales: 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
Formato: Online Artículo Texto
Lenguaje:English
Publicado: John Wiley & Sons, Ltd 2015
Materias:
Articles
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4534181/
https://www.ncbi.nlm.nih.gov/pubmed/26011795
http://dx.doi.org/10.1002/pro.2706

Internet

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4534181/
https://www.ncbi.nlm.nih.gov/pubmed/26011795
http://dx.doi.org/10.1002/pro.2706

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