MAESTRO

MAESTRO predicts changes in protein unfolding free energy (ΔΔG) caused by point mutations to assess effects on protein stability using structure-based analyses.

Key Features:

• Stability Prediction: Predicts alterations in protein unfolding free energy (ΔΔG) resulting from single point mutations.
• Scan for n‑point Mutations: Identifies the most stabilizing and destabilizing n‑point mutations with support for up to five simultaneous substitutions.
• Mutation Sensitivity Profiles: Generates mutation sensitivity profiles that quantify positional responses to amino acid substitutions.
• Disulfide Bond Evaluation: Assesses potential disulfide bonds and their effects on structural integrity.
• Versatile Structural Input: Operates on monomers, multimers, and biological assemblies as defined by the Protein Data Bank (PDB).

Scientific Applications:

• Protein Engineering: Guides selection and design of mutations to modulate protein stability based on predicted ΔΔG values.
• Structural Biology: Interprets how point mutations and disulfide changes affect structural stability using PDB-derived coordinates.
• Biotechnology: Supports identification of stability-enhancing or -reducing mutations for biotechnological applications.

Methodology:

Uses a structure-based computational approach that models protein architecture from PDB entries to predict changes in unfolding free energy upon point mutations and to evaluate potential disulfide bonds.