Protein–DNA interactions are essential for the regulations of many important
cellular processes and single mutations occurring in DNA-binding protein have profound effect on
protein-DNA interactions and are related with many diseases. SAMPDI Web Server provides fast and
accurate predictions for the effects of single amino acid substitution on the binding free energy of
protein-DNA complex. This method utilizes modified molecular mechanics Poisson-Boltzmann Surface
Area (MM/PBSA) approach along with an additional set of knowledge-based terms delivered from
investigation of the physico-chemical properties of protein-DNA complexes and results in good
agreement with experimental data.
If the usage of the server results in scientific publication, please, cite the
following papers: Link
SAMPDI is running on Clemson University's Palmetto Supercomputer Cluster.
If you experience problems, they may be due to Palmetto Cluster being not functional or under
maintenance. Contact us at email@example.com.