P.R.E.S.S.

P.R.E.S.S. performs residue-level statistical analysis of protein structural properties to quantify virtual bond lengths, bond angles, torsion angles, and residue-level statistical potentials derived from high-resolution protein structures.

Key Features:

• R package implementation: Implemented as an R package for analysis and manipulation of residue-level structural properties.
• Residue-level structural properties: Provides statistical data on virtual bond lengths, bond angles, and torsion angles for individual amino-acid residues.
• Data acquisition and surveying: Automatically downloads and surveys a large set of high-resolution protein structures.
• Statistical analysis tools: Enables querying of statistical distributions and correlations of residue-level structural properties.
• Modeling and analysis capabilities: Includes tools for modeling and analyzing specific structures based on residue-level properties.
• Residue-level statistical potentials: Computes residue-level statistical potentials to aid prediction and refinement of protein structures.
• Visualization tools: Generates Ramachandran-like plots at the residue level to visualize conformational space.

Scientific Applications:

• Structural biology: Characterizing residue conformational distributions and assessing structural stability from high-resolution structures.
• Protein engineering: Informing design and refinement of proteins using residue-level statistics and statistical potentials.
• Computational biochemistry: Supporting computational analyses of protein conformations and residue-level correlations.

Methodology:

Implemented as an R package that automatically downloads and surveys high-resolution protein structures; computes residue-level virtual bond lengths, bond angles, and torsion angles; derives statistical distributions and correlations; computes residue-level statistical potentials; performs modeling and analysis of specific structures; and generates residue-level Ramachandran-like plots.