Chapter title |
Ensemble Calculation for Intrinsically Disordered Proteins Using NMR Parameters
|
---|---|
Chapter number | 4 |
Book title |
Intrinsically Disordered Proteins Studied by NMR Spectroscopy
|
Published in |
Advances in experimental medicine and biology, January 2015
|
DOI | 10.1007/978-3-319-20164-1_4 |
Pubmed ID | |
Book ISBNs |
978-3-31-920163-4, 978-3-31-920164-1
|
Authors |
Jaka Kragelj, Martin Blackledge, Malene Ringkjøbing Jensen, Kragelj, Jaka, Blackledge, Martin, Jensen, Malene Ringkjøbing |
Abstract |
Intrinsically disordered proteins (IDPs) perform their function despite their lack of well-defined tertiary structure. Residual structure has been observed in IDPs, commonly described as transient/dynamic or expressed in terms of fractional populations. In order to understand how the protein primary sequence dictates the dynamic and structural properties of IDPs and in general to understand how IDPs function, atomic-level descriptions are needed. Nuclear magnetic resonance spectroscopy provides information about local and long-range structure in IDPs at amino acid specific resolution and can be used in combination with ensemble descriptions to represent the dynamic nature of IDPs. In this chapter we describe sample-and-select approaches for ensemble modelling of local structural propensities in IDPs with specific emphasis on validation of these ensembles. |
Mendeley readers
Geographical breakdown
Country | Count | As % |
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Unknown | 28 | 100% |
Demographic breakdown
Readers by professional status | Count | As % |
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Researcher | 12 | 43% |
Professor | 3 | 11% |
Student > Ph. D. Student | 2 | 7% |
Other | 1 | 4% |
Librarian | 1 | 4% |
Other | 2 | 7% |
Unknown | 7 | 25% |
Readers by discipline | Count | As % |
---|---|---|
Biochemistry, Genetics and Molecular Biology | 8 | 29% |
Chemistry | 5 | 18% |
Agricultural and Biological Sciences | 4 | 14% |
Materials Science | 1 | 4% |
Unknown | 10 | 36% |