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Mendeley readers
Chapter title |
Preparation of Crystalline Samples of Amyloid Fibrils and Oligomers
|
---|---|
Chapter number | 13 |
Book title |
Protein Amyloid Aggregation
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Published in |
Methods in molecular biology, January 2016
|
DOI | 10.1007/978-1-4939-2978-8_13 |
Pubmed ID | |
Book ISBNs |
978-1-4939-2977-1, 978-1-4939-2978-8
|
Authors |
Asher Moshe, Meytal Landau, David Eisenberg |
Abstract |
The molecular structures of amyloid fibers and oligomers are required in order to understand and control their formation. Yet, their partially disordered and polymorphic nature hinders structural analyses. Fortunately, short segments from amyloid proteins, which exhibit similar biophysical properties to the full-length proteins, also form fibrils and oligomers and their atomic structures can be determined. Here we describe experimental procedures used to assess fiber-forming capabilities of amyloid peptide segments and their crystallization. |
Mendeley readers
The data shown below were compiled from readership statistics for 8 Mendeley readers of this research output. Click here to see the associated Mendeley record.
Geographical breakdown
Country | Count | As % |
---|---|---|
Unknown | 8 | 100% |
Demographic breakdown
Readers by professional status | Count | As % |
---|---|---|
Student > Ph. D. Student | 4 | 50% |
Professor | 1 | 13% |
Other | 1 | 13% |
Unknown | 2 | 25% |
Readers by discipline | Count | As % |
---|---|---|
Biochemistry, Genetics and Molecular Biology | 5 | 63% |
Agricultural and Biological Sciences | 1 | 13% |
Engineering | 1 | 13% |
Unknown | 1 | 13% |