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Timeline
Mendeley readers
| Chapter title |
Methods in the Study of PTEN Structure: X-Ray Crystallography and Hydrogen Deuterium Exchange Mass Spectrometry
|
|---|---|
| Chapter number | 14 |
| Book title |
PTEN
|
| Published in |
Methods in molecular biology, January 2016
|
| DOI | 10.1007/978-1-4939-3299-3_14 |
| Pubmed ID | |
| Book ISBNs |
978-1-4939-3297-9, 978-1-4939-3299-3
|
| Authors |
Glenn R. Masson, John E. Burke, Roger L. Williams |
| 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 heterogeneity caused 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. |
Mendeley readers
The data shown below were compiled from readership statistics for 24 Mendeley readers of this research output. Click here to see the associated Mendeley record.
Geographical breakdown
| Country | Count | As % |
|---|---|---|
| Chile | 1 | 4% |
| Unknown | 23 | 96% |
Demographic breakdown
| Readers by professional status | Count | As % |
|---|---|---|
| Student > Master | 6 | 25% |
| Student > Bachelor | 4 | 17% |
| Researcher | 4 | 17% |
| Student > Ph. D. Student | 3 | 13% |
| Professor | 2 | 8% |
| Other | 3 | 13% |
| Unknown | 2 | 8% |
| Readers by discipline | Count | As % |
|---|---|---|
| Biochemistry, Genetics and Molecular Biology | 10 | 42% |
| Agricultural and Biological Sciences | 4 | 17% |
| Medicine and Dentistry | 2 | 8% |
| Pharmacology, Toxicology and Pharmaceutical Science | 1 | 4% |
| Veterinary Science and Veterinary Medicine | 1 | 4% |
| Other | 1 | 4% |
| Unknown | 5 | 21% |