AI Article Synopsis
- A new thermodynamic model has been developed to predict how well proteins can tolerate random amino acid changes.
- The model was tested using simulations of compact lattice proteins and showed strong performance in predicting outcomes.
- An approximate formula for the stability of mutant proteins, based on the number of substitutions, was derived and validated against simulation results, demonstrating good accuracy overall.
Article Abstract
We have recently proposed a thermodynamic model that predicts the tolerance of proteins to random amino acid substitutions. Here we test this model against extensive simulations with compact lattice proteins, and find that the overall performance of the model is very good. We also derive an approximate analytic expression for the fraction of mutant proteins that fold stably to the native structure, Pf(m), as a function of the number of amino acid substitutions m, and present several methods to estimate the asymptotic behavior of Pf(m) for large m. We test the accuracy of all approximations against our simulation results, and find good overall agreement between the approximations and the simulation measurements.
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Source |
|---|---|
| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1366941 | PMC |
| http://dx.doi.org/10.1529/biophysj.105.062125 | DOI Listing |
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