Effects of Mutations
Prediction of Protein Stability Changes for Single-Site Mutations from Sequences
http://www.ics.uci.edu/%7Ebaldig/mutation.html
FoldX provides a fast and quantitative estimation of the importance of the interactions contributing to the stability of proteins and protein complexes.
http://foldx.crg.es/
SIFT predicts whether an amino acid substitution affects protein function based on sequence homology and the physical properties of amino acids. SIFT can be applied to naturally occurring nonsynonymous polymorphisms and laboratory-induced missense mutations.
http://sift.bii.a-star.edu.sg/
Estimates the likelihood of a particular nonsynonymous (amino-acid changing) coding SNP to cause a functional impact on the protein. It calculates the subPSEC (substitution position-specific evolutionary conservation) score based on an alignment of evolutionarily related proteins.
http://www.pantherdb.org/tools/csnpScoreForm.jsp
CUPSAT is a tool to predict changes in protein stability upon point mutations. The prediction model uses amino acid-atom potentials and torsion angle distribution to assess the amino acid environment of the mutation site. Additionally, the prediction model can distinguish the amino acid environment using its solvent accessibility and secondary structure specificity.
http://cupsat.tu-bs.de/
SNAP is a method for evaluating effects of single amino acid substitutions on protein function. It was developed by Yana Bromberg in Rost Lab, at Columbia University, New York.
http://cubic.bioc.columbia.edu/services/SNAP/
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