CABS-flex 2.0

CABS-flex 2.0 predicts protein structural fluctuations using classical simulation techniques to characterize conformational dynamics of proteins and multimeric complexes.

Key Features:

• Scalability to larger proteins and complexes: Supports modeling of significantly larger proteins and multimeric protein complexes for fluctuation analysis.
• Customizable simulation parameters: Allows definition of distance restraints and adjustment of simulation parameters to tailor simulations.
• Contact maps integration: Produces contact maps to represent residue–residue interactions and aid interpretation of structural fluctuations.
• Single-model input and fast execution: Operates from a single protein model as input using a fast simulation approach for predicting fluctuations.
• Use of classical simulation techniques: Implements classical simulation techniques intended for efficient prediction of protein flexibility.

Scientific Applications:

• Structure–function studies: Analysis of relationships between protein structural fluctuations and protein function.
• Dynamics of large systems: Investigation of conformational dynamics in large proteins and multimeric complexes.
• Functional impact of flexibility: Assessment of how structural fluctuations influence biological processes.
• Interaction pattern analysis: Use of contact maps to study residue interaction patterns and their relation to dynamics.

Methodology:

Uses classical simulation techniques on a single protein model input, supports distance restraints, and outputs contact maps for analysis.