Predicting the Solubility of Recombinant Proteins in Escherichia coli
Abstract
We have studied the cause of inclusion body formation in Escherichia coli grown at 37 degrees C using statistical analysis of the composition of 81 proteins that do and do not form inclusion bodies. Six composition derived parameters were used. In declining order of their correlation with inclusion body formation, the parameters are charge average, turn forming residue fraction, cysteine fraction, proline fraction, hydrophilicity, and total number of residues. The correlation with inclusion body formation is strong for the first two parameters but weak for the last four. This correlation can be used to predict the probability that a protein will form inclusion bodies using only the protein's amino acid composition as the basis for the prediction.
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Cysteine residues contribute to poor solubility in the E. coli expression system.
“supporting previous findings that cysteine residues contribute to poor solubility in the E.coli expression system (Diaz et al., 2010; Wilkinson and Harrison, 1991).”
From Solubility-Weighted Index: fast and accurate prediction of protein solubility (2020) · cites this paper as Wilkinson and Harrison, 1991
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References 47 · Cited by 250
- Authors
- Wilkinson, D. L., & Harrison, R. G.
- Affiliations
- University of Oklahoma (US)
- Venue
- Nature Biotechnology
- Published
- 1991-05
- Volume
- 9
- Issue
- 5
- Pages
- 443-448
- ISSN
- 0733-222X (ISSN-L)
- 1087-0156
- 1546-1696
- OpenAlex
- W2083152645
- Cited by
- 250
- References
- 47
- Citations by year
- 2026: 2 · 2025: 4 · 2024: 6 · 2023: 5 · 2022: 7 · 2021: 5 · 2020: 6 · 2019: 6 · 2018: 11 · 2017: 8 · 2016: 5 · 2015: 7 · 2014: 13 · 2013: 19 · 2012: 11
- FWCI
- 1.70
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Nature Biotechnology (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein purification and stability
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Machine Learning in Bioinformatics
- Keywords
- recombinant protein solubility, inclusion bodies, Escherichia coli, amino acid composition, protein folding, hydrophobicity, protein charge, cysteine content, proline content, solubility prediction
- MeSH terms
- Amino Acids, Animals, Escherichia coli, Humans, Probability, Recombinant Proteins, Solubility, Temperature, Models, Statistical
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