Predicting recombinant protein expression experiments using molecular dynamics simulation

摘要: Abstract Soluble expression of de novo-designed proteins in Escherichia coli (E. coli) remains empirical. For given experimental conditions success is determined part by protein primary sequence. This has been previously explored with varying using a variety statistical solubility prediction tools though without taking fold stability into account. In the present study, three-dimensional structure molecular dynamics (MD) simulations used to predict as new approach set four-helix bundles. Stability-related parameters for ten structures were thermal unfolding MD simulation and build models support vector machine (SVM) classifier. The most accurate identified their performance on five independent bundle sequences. final model provided classification this test was successfully applied challenge two newly designed combination simulation-derived an SVM classifier potential recombinant outcome With further development, utilizing higher-dimensional structural information may have advance biotechnology through modern computational science.