Your browser doesn't support javascript.
loading
Show: 20 | 50 | 100
Results 1 - 2 de 2
Filter
Add more filters










Database
Language
Publication year range
1.
BMC Bioinformatics ; 21(Suppl 2): 80, 2020 Mar 11.
Article in English | MEDLINE | ID: mdl-32164574

ABSTRACT

BACKGROUND: Interactions between proteins and non-proteic small molecule ligands play important roles in the biological processes of living systems. Thus, the development of computational methods to support our understanding of the ligand-receptor recognition process is of fundamental importance since these methods are a major step towards ligand prediction, target identification, lead discovery, and more. This article presents visGReMLIN, a web server that couples a graph mining-based strategy to detect motifs at the protein-ligand interface with an interactive platform to visually explore and interpret these motifs in the context of protein-ligand interfaces. RESULTS: To illustrate the potential of visGReMLIN, we conducted two cases in which our strategy was compared with previous experimentally and computationally determined results. visGReMLIN allowed us to detect patterns previously documented in the literature in a totally visual manner. In addition, we found some motifs that we believe are relevant to protein-ligand interactions in the analyzed datasets. CONCLUSIONS: We aimed to build a visual analytics-oriented web server to detect and visualize common motifs at the protein-ligand interface. visGReMLIN motifs can support users in gaining insights on the key atoms/residues responsible for protein-ligand interactions in a dataset of complexes.


Subject(s)
Ligands , Proteins/metabolism , User-Computer Interface , Humans , Hydrogen Bonding , Hydrophobic and Hydrophilic Interactions , Protein Binding , Proteins/chemistry
2.
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
SELECTION OF CITATIONS
SEARCH DETAIL
...