DSSPcont

DSSPcont produces continuous residue-level secondary structure assignments by averaging multiple DSSP outputs computed from PDB three-dimensional coordinates with varying hydrogen-bond thresholds to capture thermal-induced conformational variability.

Key Features:

• Continuous assignment approach: Calculates weighted averages over ten discrete DSSP assignments computed with varying hydrogen-bond thresholds to produce a continuum of secondary structure values per residue expressed as percentage likelihoods across the eight DSSP states.
• Reflection of thermal fluctuations: Captures structural variations induced by thermal fluctuations as observed in Nuclear Magnetic Resonance (NMR) data.
• Single-model reproduction of NMR variability: Reproduces structural variations seen across multiple NMR models from a single X-ray structure, enabling extraction of functionally relevant variations from crystallographic coordinates.

Scientific Applications:

• Understanding protein flexibility: Provides residue-level probability distributions of the eight DSSP states to analyze conformational variability and flexibility.
• Drug design and development: Reveals dynamic secondary-structure states that can expose transient or alternative binding-site conformations relevant for ligand design.
• Comparative structural analysis: Facilitates comparison of conformational ensembles and evolutionary or functional adaptations by quantifying secondary-structure variability.

Methodology:

Compute ten DSSP assignments from PDB three-dimensional coordinates using varying hydrogen-bond thresholds and combine them via weighted averaging to yield residue-level percentage likelihoods across the eight DSSP states.