Glutton

Glutton generates structural ensembles of partly disordered proteins from nuclear magnetic resonance (NMR) chemical shifts (CS) to characterize conformational distributions and inform folding and structure refinement.

Key Features:

• Database Integration: Links chemical shifts (CS) from NMR experiments to protein 3D structures via a database of over 5,270 entries organized into three hierarchical levels.
• Statistical Analysis: Generates statistical distributions of ϕ-ψ dihedral angles from chemical shifts and can operate in the reverse direction (inferring chemical shifts from ϕ-ψ distributions).
• Structural Ensemble Generation: Calculates structural ensembles that represent the range of conformations accessible to partly disordered proteins based on ϕ-ψ angle distributions derived from chemical shifts.
• Refinement Capabilities: Produces ensembles that serve as initial models for refinement using additional experimental restraints or computational methods for folded proteins.

Scientific Applications:

• Protein dynamics and folding: Characterizes conformational flexibility and folding mechanisms of partly disordered proteins using chemical shift–derived ensembles.
• Structure determination and prediction: Supplies initial ensemble models to improve structure determination and prediction for folded proteins via subsequent refinement.
• Interaction studies: Supports analysis of folding-upon-binding and interaction-induced conformational changes by providing ensemble representations from chemical shifts.

Methodology:

Links NMR chemical shifts (CS) to protein 3D structures, computes ϕ-ψ dihedral angle distributions from chemical shifts (and vice versa), generates structural ensembles from those distributions, and provides ensembles for refinement with additional experimental restraints or computational methods.