Chapter title |
Native Mass Spectrometry for the Characterization of Structure and Interactions of Membrane Proteins
|
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Chapter number | 11 |
Book title |
Membrane Protein Structure and Function Characterization
|
Published in |
Methods in molecular biology, January 2017
|
DOI | 10.1007/978-1-4939-7151-0_11 |
Pubmed ID | |
Book ISBNs |
978-1-4939-7149-7, 978-1-4939-7151-0
|
Authors |
Jeroen F. van Dyck, Albert Konijnenberg, Frank Sobott |
Abstract |
Over the past years, native mass spectrometry and ion mobility have grown into techniques that are widely applicable to the study of aspects of protein structure. More recently, it has become apparent that this approach provides a very promising avenue for the investigation of integral membrane proteins in lipid or detergent environments.In this chapter, we discuss applications of native mass spectrometry and ion mobility in membrane protein research-what is important to take into consideration when working with membrane proteins, and what the requirements are for sample preparation for native mass spectrometry. Furthermore, we will discuss the types of information provided by the measurements, including the oligomeric state, subunit composition and stoichiometry, interactions with detergents or lipids, conformational transitions, and the binding and structural effect of ligands and drugs. |
Mendeley readers
Geographical breakdown
Country | Count | As % |
---|---|---|
Unknown | 19 | 100% |
Demographic breakdown
Readers by professional status | Count | As % |
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Student > Ph. D. Student | 7 | 37% |
Researcher | 4 | 21% |
Student > Bachelor | 2 | 11% |
Student > Master | 1 | 5% |
Unknown | 5 | 26% |
Readers by discipline | Count | As % |
---|---|---|
Biochemistry, Genetics and Molecular Biology | 10 | 53% |
Agricultural and Biological Sciences | 2 | 11% |
Chemistry | 1 | 5% |
Neuroscience | 1 | 5% |
Unknown | 5 | 26% |