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Protein Mutational Analysis Bioinformatics.

Bioinformatic Tools are able to predict a protein's structure either in 2-dimensions (2-D) or three-dimensions (3-D). This may not be a real representation of the actual structure of a protein, however it is a good starting point to predict enzymatic pockets, and protein-protein interaction domains. After prediction, confirmation of protein structure can be made using X-ray Crystallography techniques.

Bioinformatic Programs Used to Protein Mutations:

Correlated Protein Mutations Analysis of correlated mutations

MutaProt: Comparison of PDB files which differ by point mutations

Databases for Protein Mutations - Use these database to search for known protein mutations:

PMD: Protein Mutant Database

PMR: Protein Mutant Resources

HGVS: Human Genome Variation Society

Single Nucleotide Polymorphisms for Biomedical Research: SNP Consortium

Single Nucleotide Polymorphisms Entrez Pubmed Text Name Search

Bioinformatic Tools can predict the effect of mutations on secondary structure and protein function. You can compare the results of the wild-type protein to the mutant protein and examine predicted possible effects of the mutation.

Furthermore, experimental data is needed to confirm any bioinformatic prediction of protein mutants. This can be done by examining key residues in protein function or protein interaction domains using Ala (alanine) substitution and analyze the experimental data which results.


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