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Mendeley readers
| Chapter title |
Preparation of Amyloid Fibrils for Magic-Angle Spinning Solid-State NMR Spectroscopy
|
|---|---|
| Chapter number | 11 |
| Book title |
Protein Amyloid Aggregation
|
| Published in |
Methods in molecular biology, January 2016
|
| DOI | 10.1007/978-1-4939-2978-8_11 |
| Pubmed ID | |
| Book ISBNs |
978-1-4939-2977-1, 978-1-4939-2978-8
|
| Authors |
Marcus D. Tuttle, Joseph M. Courtney, Alexander M. Barclay, Chad M. Rienstra |
| Abstract |
Solid-state NMR spectroscopy (SSNMR) is an established and invaluable tool for the study of amyloid fibril structure with atomic-level detail. Optimization of the homogeneity and concentration of fibrils enhances the resolution and sensitivity of SSNMR spectra. Here, we present a fibrillization and fibril processing protocol, starting from purified monomeric α-synuclein, that enables the collection of high-resolution SSNMR spectra suitable for site-specific structural analysis. This protocol does not rely on any special features of α-synuclein and should be generalizable to any other amyloid protein. |
Mendeley readers
The data shown below were compiled from readership statistics for 9 Mendeley readers of this research output. Click here to see the associated Mendeley record.
Geographical breakdown
| Country | Count | As % |
|---|---|---|
| Unknown | 9 | 100% |
Demographic breakdown
| Readers by professional status | Count | As % |
|---|---|---|
| Professor | 3 | 33% |
| Student > Ph. D. Student | 2 | 22% |
| Librarian | 1 | 11% |
| Unspecified | 1 | 11% |
| Researcher | 1 | 11% |
| Other | 1 | 11% |
| Readers by discipline | Count | As % |
|---|---|---|
| Biochemistry, Genetics and Molecular Biology | 3 | 33% |
| Chemistry | 3 | 33% |
| Agricultural and Biological Sciences | 1 | 11% |
| Unspecified | 1 | 11% |
| Unknown | 1 | 11% |