The DOI matches its Crossref record; 55 of the 55 references it cites were found in a registry or an index.
How to Get Insight into Amyloid Structure and Formation from Infrared Spectroscopy
Open accessAbstract
There is an enormous amount of interest in the structures and formation mechanisms of amyloid fibers. In this Perspective, we review the most common structural motifs of amyloid fibers and discuss how infrared spectroscopy and isotope labeling can be used to identify their structures and aggregation kinetics. We present three specific strategies, site-specific labeling to obtain residue-by-residue structural information, isotope dilution of uniformly labeled proteins for identifying structural folds and protein mixtures, and expressed protein ligation for studying the domain structures of large proteins. For each of these methods, vibrational couplings are the source of the identifying features in the infrared spectrum. Examples are provided using the proteins hIAPP, Aβ, polyglutamine, and γD-crystallin. We focus on FTIR spectroscopy but also describe new observables made possible by 2D IR spectroscopy.
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Cites
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Molecular chaperones in protein folding and proteostasis
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Structure of the cross-β spine of amyloid-like fibrils
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Concepts and Methods of 2D Infrared Spectroscopy
Hamm, P., & Zanni, M. (2011) · Cambridge University Press eBooks · doi:10.1017/cbo9780511675935 · Cited by 1,364
Self-citationFunctional amyloid – from bacteria to humans
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Experimental Constraints on Quaternary Structure in Alzheimer's β-Amyloid Fibrils
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Amyloid Fibrils of the HET-s(218–289) Prion Form a β Solenoid with a Triangular Hydrophobic Core
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Identifying the amylome, proteins capable of forming amyloid-like fibrils
Goldschmidt, L., Teng, P. K., Riek, R., & Eisenberg, D. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0915166107 · Cited by 809
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Cited by
Roeters, S. J., Iyer, A., Pletikapić, G., Kogan, V., Subramaniam, V., & Woutersen, S. (2017) · Scientific Reports · doi:10.1038/srep41051 · Cited by 146
Exploring a diverse world of effector domains and amyloid signaling motifs in fungal NLR proteins
Wojciechowski, J. W., Tekoglu, E., Gąsior-Głogowska, M., Coustou, V., Szulc, N., Szefczyk, M., Kopaczyńska, M., Saupe, S. J., & Dyrka, W. (2022) · PLOS Computational Biology · doi:10.1371/journal.pcbi.1010787 · Cited by 19
Biomimetic supramolecular protein matrix restores structure and properties of human dental enamel
Hasan, A., Chuvilin, A., Van Teijlingen, A., Rouco, H., Parmenter, C., Venturi, F., Fay, M., Greco, G., Pugno, N. M., Ruben, J., et al. (2025) · Nature Communications · doi:10.1038/s41467-025-64982-y · Cited by 15
Metadata
- Authors
- Moran, S. D., & Zanni, M. T.
- Venue
- The Journal of Physical Chemistry Letters
- Publisher
- American Chemical Society (ACS)
- Published
- 2014-05-22
- Volume
- 5
- Issue
- 11
- Pages
- 1984-1993
- ISSN
- 1948-7185 (ISSN-L)
- OpenAlex
- W2330959820
- Cited by
- 264
- References
- 55
- FWCI
- 8.57
- Type
- journal article
- Language
- en
- Open access
- hybrid
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
