ssPINE

ssPINE automates probabilistic backbone and side-chain chemical shift assignment from solid-state NMR peak lists to support protein structural determination.

Key Features:

• Automated Assignment: Processes peak lists from solid-state NMR experiments to assign backbone and side-chain chemical shifts.
• Probabilistic Algorithm: Uses a probabilistic algorithm to evaluate assignment possibilities and produce automated assignments.
• Input Requirements: Accepts protein sequence and peak lists and accommodates data from different isotopic compositions and labeling schemes.
• ssNMR Experiment Support: Handles peak lists derived from various solid-state NMR experiments.
• Technological Integration: Integrates data considerations from non-uniform sampling, faster magic angle spinning, and innovative pulse sequences to enable analysis of large biomolecules including membrane proteins.

Scientific Applications:

• Structure determination of large and complex proteins: Facilitates chemical shift assignment for proteins that are challenging for solution NMR due to molecular weight or complexity.
• Membrane protein analysis: Supports assignment workflows for membrane proteins and other intricate protein systems studied by solid-state NMR.

Methodology:

Applies a probabilistic algorithm that processes protein sequence and solid-state NMR peak lists to generate automated backbone and side-chain chemical shift assignments while accommodating different isotopic compositions.