Protein NMR Spectroscopy: 2D HSQC Spectra of Folded vs. Unfolded Protein

A figure illustrating the relationship between 2D 1H-15N HSQC NMR spectra for folded and unfolded states of a specific protein. The data includes spectra for a folded 2x10 kDa dimer and its unfolded monomer, with a specific residue signal circled for comparison. The figure also references the PDB structure 4mjh and a model from the Protein Ensemble Database PED1AAD.

Use Cases

• Compare NMR signal dispersion patterns between folded and unfolded protein states based on the described 2D HSQC spectra.
• Analyze the relationship between protein secondary structure (alpha-helix vs. beta-strand) and proton dimension signal dispersion as mentioned in the description.
• Benchmark computational models of intrinsically disordered proteins against the provided structural model from PED1AAD.
• Study the spectral changes of a specific amino acid residue (S156) across different protein conformational states.

Strengths

• Provides a direct visual comparison of NMR spectra for two distinct protein states (folded dimer and unfolded monomer).
• References specific, verifiable structural data sources (PDB ID 4mjh and Protein Ensemble Database entry PED1AAD).
• Highlights a specific, annotated spectral feature (circled resonance from S156) for detailed analysis.

Limitations

• The dataset appears to be a single illustrative figure; the underlying spectral data files and their scale are unknown.
• Column-level documentation and sample data are unavailable, limiting reproducibility and quantitative analysis.
• Last update date and dataset size are unknown, which may affect suitability assessment.

Provenance

Source

paperswithcode, authored by T. Reid Alderson.

Collection Method

Likely contains NMR spectroscopy data and structural models from public databases (PDB, PED).