Fodis

Fodis analyzes force-distance curves from single-molecule force spectroscopy (SMFS) experiments to standardize processing, classify unfolding pathways, and detect structural heterogeneity in protein folding studies.

Key Features:

• Automatic Processing: Performs near-fully automated processing of raw SMFS force-distance curves to enhance reproducibility.
• Comprehensive Analysis: Extracts and interprets mechanical information from force-distance curves to characterize protein mechanical properties.
• Classification of Unfolding Pathways: Classifies potential protein unfolding pathways from force-distance data to elucidate folding and unfolding mechanisms.
• Identification of Structural Heterogeneity: Detects and characterizes structural heterogeneities observed during protein unfolding events.

Scientific Applications:

• Protein Folding Dynamics: Analyzes single-molecule unfolding events to study protein folding and unfolding mechanisms using SMFS data.
• Structural Biology Research: Characterizes conformational heterogeneity and unfolding landscapes relevant to structural biology studies of proteins.
• Biophysical Studies: Provides quantitative insights into mechanical properties and force-dependent behaviors of biomolecules from force spectroscopy data.

Methodology:

Applies a standardized processing pipeline for SMFS force-distance curves using automated algorithms and a classification system to categorize unfolding events and structural variations.