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Lyophilization-induced reversible changes in the secondary structure of proteins.
Open accessAbstract
Changes in the secondary structure of some dozen different proteins upon lyophilization of their aqueous solutions have been investigated by means of Fourier-transform infrared spectroscopy in the amide III band region. Dehydration markedly (but reversibly) alters the secondary structure of all the proteins studied, as revealed by both the quantitative analysis of the second derivative spectra and the Gaussian curve fitting of the original infrared spectra. Lyophilization substantially increases the beta-sheet content and lowers the alpha-helix content of all proteins. In all but one case, proteins become more ordered upon lyophilization.
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Cited by
Strategies for Stabilization of Enzymes in Organic Solvents
Stepankova, V., Bidmanova, S., Koudelakova, T., Prokop, Z., Chaloupkova, R., & Damborsky, J. (2013) · ACS Catalysis · doi:10.1021/cs400684x · Cited by 659
Zhang, X., Yu, Q., Wang, Y.-A., & Zhao, J. (2018) · International Journal of Nanomedicine · doi:10.2147/ijn.s150875 · Cited by 25
Metadata
- Authors
- Griebenow, K., & Klibanov, A. M.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 1995-11-21
- Volume
- 92
- Issue
- 24
- Pages
- 10969-10976
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2075791526
- Cited by
- 369
- References
- 0
- FWCI
- 3.67
- Type
- journal article
- Language
- en
- Open access
- green
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- CoChat. (2026). Citation check: Lyophilization-induced reversible changes in the secondary structure of proteins. https://app.cochat.ai/papers/10.1073/pnas.92.24.10969
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- Griebenow, K., & Klibanov, A. M. (1995). Lyophilization-induced reversible changes in the secondary structure of proteins. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.92.24.10969
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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