SDM: a server for predicting effects of mutations on protein stability

Here, we report a webserver for the improved SDM, used for predicting the effects of mutations on protein stability. As a pioneering knowledge-based approach, SDM has been highlighted as the most appropriate method to use in combination with many other approaches. We have updated the environment-specific amino-acid substitution tables based on the current expanded PDB (a 5-fold increase in information), and introduced new residue-conformation and interaction parameters, including packing density and residue depth. The updated server has been extensively tested using a benchmark containing 2690 point mutations from 132 different protein structures. The revised method correlates well against the hypothetical…

• BA
  Bill and Melinda Gates Foundation
• WT
  Wellcome Trust

  Award: 093167/Z/10/Z
• RC
  Research Councils UK
• CN
  Conselho Nacional das Fundações Estaduais de Amparo à Pesquisa
• MR
  Medical Research Council

  Awards: MR/N501864/1, MR/M026302/1
• NH
  National Health and Medical Research Council

  Award: APP1072476