The DOI matches its Crossref record; 54 of the 54 references it cites were found in a registry or an index.
Determining Beta-Sheet Crystallinity in Fibrous Proteins by Thermal Analysis and Infrared Spectroscopy
Abstract
We report a study of self-assembled beta-pleated sheets in B. mori silk fibroin films using thermal analysis and infrared spectroscopy. B. mori silk fibroin may stand as an exemplar of fibrous proteins containing crystalline beta-sheets. Materials were prepared from concentrated solutions (2−5 wt % fibroin in water) and then dried to achieve a less ordered state without beta-sheets. Crystallization of beta-pleated sheets was effected either by heating the films above the glass transition temperature ( T g ) and holding isothermally or by exposure to methanol. The fractions of secondary structural components including random coils, alpha-helices, beta-pleated sheets, turns, and side chains were evaluated using Fourier self-deconvolution (FSD) of the infrared absorbance spectra. The silk fibroin films were studied thermally using temperature-modulated differential scanning calorimetry (TMDSC) to obtain the reversing heat capacity. The increment of the reversing heat capacity Δ C p 0 ( T g ) at the glass transition for the less ordered, noncrystalline, silk fibroin is found to be 0.478 ± 0.005 J/(g K). As crystalline beta-sheets form, the heat capacity increment at T g is systematically decreased. We find that the heat capacity increment from the TMDSC trace is linearly well correlated (negatively) with beta-sheet content φ C determined from FSD, yielding Δ C p = 0.475−0.494φ C . The correlation allows the beta-sheet content to be determined from a direct measurement of the heat capacity increment at T g . This type of analysis can serve as an alternative to X-ray methods and may have wide applicability to other crystalline beta-sheet forming proteins.
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Cites
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Self-citationRegulation of Silk Material Structure by Temperature-Controlled Water Vapor Annealing
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Raia, N. R., Partlow, B. P., McGill, M., Kimmerling, E. P., Ghezzi, C. E., & Kaplan, D. L. (2017) · Biomaterials · doi:10.1016/j.biomaterials.2017.03.046 · Cited by 312
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Cho, S. Y., Yun, Y. S., Lee, S., Jang, D., Park, K.-Y., Kim, J. K., Kim, B. H., Kang, K., Kaplan, D. L., & Jin, H.-J. (2015) · Nature Communications · doi:10.1038/ncomms8145 · Cited by 277
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Metadata
- Authors
- Hu, X., Kaplan, D., & Cebe, P.
- Venue
- Macromolecules
- Publisher
- American Chemical Society (ACS)
- Published
- 2006-08-11
- Volume
- 39
- Issue
- 18
- Pages
- 6161-6170
- ISSN
- 0024-9297 (ISSN-L)
- 1520-5835
- OpenAlex
- W2595614671
- Cited by
- 1,251
- References
- 54
- FWCI
- 5.24
- Type
- journal article
- Language
- en
- Open access
- closed
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