CoRINs

CoRINs compares residue interaction networks (RINs) derived from protein structures to quantify and visualize differences in amino acid residue interactions that underlie conformational variation and mutation effects.

Key Features:

• Comparison of Multiple RINs: Compares RINs from different protein structures to identify changes in residue-level interactions and network topology.
• Visualization of RIN Comparisons: Generates tables and graphics that represent comparative relationships among residues and interactions.
• Network Parameter Summarization: Summarizes differences in various network parameters across RINs to enable quantitative assessment of structural variation.

Scientific Applications:

• Protein Conformational Variation Evaluation: Assesses how different conformations affect residue interactions and structure-function relationships.
• Model Validation: Provides comparative RIN analysis to validate homology models against experimental structures by checking consistency of residue interactions.
• Mutation Impact Assessment: Identifies changes in RINs caused by amino acid substitutions to predict potential impacts on protein structure and activity relevant to genetic diseases and drug design.

Methodology:

Constructs RINs using graph theory with nodes as amino acid residues and edges representing interactions with structural elements, then compares those networks across protein structures and highlights differences in network parameters through visualizations.