@inbook{54278e287c084d23bad440f3fd8fc8c9,
title = "Methods in the study of PTEN structure: X-ray crystallography and hydrogen deuterium exchange mass spectrometry",
abstract = "Despite its small size and deceptively simple domain organization, PTEN remains a challenging structural target due to its N- and C-terminal intrinsically disordered segments, and the conformational heterogeneitycaused by phosphorylation of its C terminus. Using hydrogen/deuterium exchange mass spectrometry (HDX-MS), it is possible to probe the conformational dynamics of the disordered termini, and also to determine how PTEN binds to lipid membranes. Here, we describe how to purify recombinant, homogenously dephosphorylated PTEN from a eukaryotic system for subsequent investigation with HDX-MS or crystallography.",
keywords = "HDX-MS, Insect cell expression, Liposomeb preparation, Mass spectrometry, Protein purification",
author = "Masson, {Glenn R.} and Burke, {John E.} and Williams, {Roger L.}",
note = "Publisher Copyright: {\textcopyright} Springer Science+Business Media New York 2016.",
year = "2016",
doi = "10.1007/978-1-4939-3299-3_14",
language = "English",
isbn = "978-1-4939-3297-9",
series = "Methods in Molecular Biology",
publisher = "Humana Press",
pages = "215--230",
editor = "Leonardo Salmena and Vuk Stambolic",
booktitle = "PTEN",
address = "United States",
}