You are seeing a free-to-access but limited selection of the activity Altmetric has collected about this research output.
Click here to find out more.
Mendeley readers
Chapter title |
Quenched Hydrogen Exchange NMR of Amyloid Fibrils
|
---|---|
Chapter number | 14 |
Book title |
Protein Amyloid Aggregation
|
Published in |
Methods in molecular biology, January 2016
|
DOI | 10.1007/978-1-4939-2978-8_14 |
Pubmed ID | |
Book ISBNs |
978-1-4939-2977-1, 978-1-4939-2978-8
|
Authors |
Andrei T. Alexandrescu |
Abstract |
Amyloid fibrils are associated with a number of human diseases. These aggregatively misfolded intermolecular β-sheet assemblies constitute some of the most challenging targets in structural biology because to their complexity, size, and insolubility. Here, protocols and controls are described for experiments designed to study hydrogen-bonding in amyloid fibrils indirectly, by transferring information about amide proton occupancy in the fibrils to the dimethyl sulfoxide-denatured state. Since the denatured state is amenable to solution NMR spectroscopy, the method can provide residue-level-resolution data on hydrogen exchange for the monomers that make up the fibrils. |
Mendeley readers
The data shown below were compiled from readership statistics for 10 Mendeley readers of this research output. Click here to see the associated Mendeley record.
Geographical breakdown
Country | Count | As % |
---|---|---|
Unknown | 10 | 100% |
Demographic breakdown
Readers by professional status | Count | As % |
---|---|---|
Student > Bachelor | 3 | 30% |
Unspecified | 2 | 20% |
Student > Doctoral Student | 1 | 10% |
Professor | 1 | 10% |
Student > Ph. D. Student | 1 | 10% |
Other | 1 | 10% |
Unknown | 1 | 10% |
Readers by discipline | Count | As % |
---|---|---|
Biochemistry, Genetics and Molecular Biology | 4 | 40% |
Pharmacology, Toxicology and Pharmaceutical Science | 1 | 10% |
Unspecified | 1 | 10% |
Materials Science | 1 | 10% |
Neuroscience | 1 | 10% |
Other | 0 | 0% |
Unknown | 2 | 20% |