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.
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Acknowledgements
We thank our coworkers for their contributions to development of these methods, and NIH (AG029430 & SG04812), DOE (DE-FC02-02ER63421), and NSF (MCB-0958111) for support. DE and ML thank the U.S.-Israel Binational Science Foundation (BSF). ML thanks the Alon Fellowship from the Israeli Council for Higher Education, the I-CORE Program of the Planning and Budgeting Committee and The Israel Science Foundation, Center of Excellence in Integrated Structural Cell Biology; Grant No 1775/12, the Support for training and career development of researchers (Marie Curie) CIG, Seventh framework program, Single Benefi ciary, the J. and A. Taub Biological Research Fund, and the David and Inez Mayers Career Advancement Chair in Life Sciences.
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Moshe, A., Landau, M., Eisenberg, D. (2016). Preparation of Crystalline Samples of Amyloid Fibrils and Oligomers. In: Eliezer, D. (eds) Protein Amyloid Aggregation. Methods in Molecular Biology, vol 1345. Humana Press, New York, NY. https://doi.org/10.1007/978-1-4939-2978-8_13
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DOI: https://doi.org/10.1007/978-1-4939-2978-8_13
Publisher Name: Humana Press, New York, NY
Print ISBN: 978-1-4939-2977-1
Online ISBN: 978-1-4939-2978-8
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