bioRxiv · 10.1101/2020.02.15.951012
Protein solubility is controlled by global structural flexibility
Abstract
MotivationRecombinant protein production is a widely used technique in the biotechnology and biomedical industries, yet only a quarter of target proteins are soluble and can therefore be purified. ResultsWe have discovered that global structural flexibility, which can be modeled by normalised B-factors, accurately predicts the solubility of 12,216 recombinant proteins expressed in Escherichia coli. We have optimised B-factors, and derived a new set of values for solubility scoring that further improves prediction accuracy. We call this new predictor the Solubility-Weighted Index (SWI). Importantly, SWI outperforms many existing protein solubility prediction tools. Furthermore, we have developed SoDoPE (Soluble Domain for Protein Expression), a web interface that allows users to choose a protein region of interest for predicting and maximising both protein expression and solubility. AvailabilityThe SoDoPE web server and source code are freely available at https://tisigner.com/sodope and https://github.com/Gardner-BinfLab/TISIGNER-ReactJS, respectively. The code and data for reproducing our analysis can be found at https://github.com/Gardner-BinfLab/SoDoPE_paper2020.
Source connections
Explore related subjects
Keep this discovery
Explore connections, maps & timelines
Bhandari, B. K., Gardner, P. P., Lim, C. S.. 2020-02-16. Protein solubility is controlled by global structural flexibility. https://doi.org/10.1101/2020.02.15.951012
Cite the original work for its findings. Save a collection to share your selection of sources.