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BMC Bioinformatics ; 18(Suppl 10): 403, 2017 Sep 13.
Article in English | MEDLINE | ID: mdl-28929973

ABSTRACT

BACKGROUND: A huge amount of data about genomes and sequence variation is available and continues to grow on a large scale, which makes experimentally characterizing these mutations infeasible regarding disease association and effects on protein structure and function. Therefore, reliable computational approaches are needed to support the understanding of mutations and their impacts. Here, we present VERMONT 2.0, a visual interactive platform that combines sequence and structural parameters with interactive visualizations to make the impact of protein point mutations more understandable. RESULTS: We aimed to contribute a novel visual analytics oriented method to analyze and gain insight on the impact of protein point mutations. To assess the ability of VERMONT to do this, we visually examined a set of mutations that were experimentally characterized to determine if VERMONT could identify damaging mutations and why they can be considered so. CONCLUSIONS: VERMONT allowed us to understand mutations by interpreting position-specific structural and physicochemical properties. Additionally, we note some specific positions we believe have an impact on protein function/structure in the case of mutation.


Subject(s)
DNA Mutational Analysis/methods , Software , Amino Acid Sequence , Conserved Sequence/genetics , Humans , Hydrophobic and Hydrophilic Interactions , Mutation/genetics , Polymorphism, Single Nucleotide/genetics , Sequence Alignment , Tumor Suppressor Protein p53/chemistry , Tumor Suppressor Protein p53/genetics
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