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Native-like Secondary Structure in Interleukin-1.beta. Inclusion Bodies by Attenuated Total Reflectance FTIR
Abstract
Attenuated total reflectance FTIR has been used to study the structure of human interleukin-1 beta in inclusion bodies (IBs) and other aggregated forms. The secondary structure composition of native wild-type IL-1 beta determined by FTIR is in excellent agreement with that previously determined by crystallography and NMR: 52% beta-sheet, 25% loop/irregular structure, and 23% turn. Remarkably, IL-1 beta inclusion bodies exhibit secondary structural composition very similar to that of the native protein. The results indicate that the IBs form from a folding intermediate that has nativelike secondary structure. The secondary structure content of aggregated IL-1 beta, formed either in refolding or by thermal denaturation, was identical within experimental error to that of the IB, indicating that these aggregates were formed from intermediates with structures similar to that of the inclusion body.
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Citations
Cites
Protein secondary structures in water from second-derivative amide I infrared spectra
Dong, A., Huang, P., & Caughey, W. S. (1990) · Biochemistry · doi:10.1021/bi00465a022 · Cited by 1,333
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Recombinant protein folding and misfolding in Escherichia coli
Baneyx, F., & Mujacic, M. (2004) · Nature Biotechnology · doi:10.1038/nbt1029 · Cited by 1,445
Protein aggregation: folding aggregates, inclusion bodies and amyloid
Fink, A. L. (1998) · Folding and Design · doi:10.1016/s1359-0278(98)00002-9 · Cited by 1,157
Self-citationEvidence for a Partially Folded Intermediate in α-Synuclein Fibril Formation
Uversky, V. N., Li, J., & Fink, A. L. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m010907200 · Cited by 1,096
Self-citationFTIR reveals structural differences between native β‐sheet proteins and amyloid fibrils
Zandomeneghi, G., Krebs, M. R. H., McCammon, M. G., & Fändrich, M. (2004) · Protein Science · doi:10.1110/ps.041024904 · Cited by 725
Protein recovery from inclusion bodies of Escherichia coli using mild solubilization process
Singh, A., Upadhyay, V., Upadhyay, A. K., Singh, S. M., & Panda, A. K. (2015) · Microbial Cell Factories · doi:10.1186/s12934-015-0222-8 · Cited by 444
Metadata
- Authors
- Oberg, K., Chrunyk, B. A., Wetzel, R., & Fink, A. L.
- Venue
- Biochemistry
- Publisher
- American Chemical Society (ACS)
- Published
- 1994-03-01
- Volume
- 33
- Issue
- 9
- Pages
- 2628-2634
- ISSN
- 0006-2960 (ISSN-L)
- 1520-4995
- OpenAlex
- W1992626528
- Cited by
- 202
- References
- 1
- FWCI
- 2.45
- Type
- journal article
- Language
- en
- Open access
- closed
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- CoChat. (2026). Citation check: Native-like Secondary Structure in Interleukin-1.beta. Inclusion Bodies by Attenuated Total Reflectance FTIR. https://app.cochat.ai/papers/10.1021/bi00175a035
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- Oberg, K., Chrunyk, B. A., Wetzel, R., & Fink, A. L. (1994). Native-like Secondary Structure in Interleukin-1.beta. Inclusion Bodies by Attenuated Total Reflectance FTIR. Biochemistry. https://doi.org/10.1021/bi00175a035
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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.
