Assessing computational methods for predicting protein stability upon mutation: good on average but not in the details.

Abstract

Methods for protein modeling and design advanced rapidly in recent years. At the heart of these computational methods is an energy function that calculates the free energy of the system. Many of these functions were also developed to estimate the consequence of mutation on protein stability or binding affinity. In the current study, we chose six different… (More)
DOI: 10.1093/protein/gzp030

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Cite this paper

@article{Potapov2009AssessingCM, title={Assessing computational methods for predicting protein stability upon mutation: good on average but not in the details.}, author={Vladimir Potapov and Mati Cohen and Gideon Schreiber}, journal={Protein engineering, design & selection : PEDS}, year={2009}, volume={22 9}, pages={553-60} }