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

ABSTRACT: 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 reverse mutations, better than comparable methods built using machine-learning appro

SUBMITTER: Pandurangan AP 

PROVIDER: S-EPMC5793720 | biostudies-literature | 2017 Jul

REPOSITORIES: biostudies-literature