icorrelationplus

icorrelationplus extracts and analyzes dynamical pairwise correlations in proteins from molecular dynamics (MD) trajectories and normal-mode analyses of coarse-grained models to elucidate residue coupling and functional relationships.

Key Features:

• Calculation of Pairwise Correlations: Computes pairwise dynamical correlations between residues from large MD trajectories and normal-mode analyses of coarse-grained models.
• Correlation Map Visualization: Produces correlation maps to represent residue-residue dynamical couplings for interpretation of protein dynamics.
• Identification of Key Residues: Identifies residues with strong dynamical coupling that may contribute to allosteric regulation or functional effects of mutations.
• Integration with Sequence Coevolution Data: Enables combination and comparison of dynamical correlation data with sequence coevolution information.

Scientific Applications:

• Allosteric Regulation Studies: Detects long-distance dynamical couplings and residues implicated in transmission of allosteric signals.
• Protein Function Analysis: Assists in dissecting the functional implications of residue interactions and mutational effects on dynamics.
• Comparative Dynamics and Evolution: Compares dynamical coupling patterns with evolutionary sequence coevolution to link dynamics and conservation.

Methodology:

Extracts correlation data from extensive MD simulations and from normal-mode analyses of coarse-grained models to examine residue interactions.