FOR005: Immunoglobulin Light Chain Protein Aggregation Pathway from NMR Spectroscopy

Solution-state NMR spectroscopy data tracks the misfolding pathway of the patient-derived λ-III light chain variable domain FOR005 at atomic resolution. The dataset, associated with an Open Access paper by Tejaswini Pradhan, compares the wild-type protein with a single-point mutant and the closest germline protein. It provides mechanistic insights into how mutations induce partial unfolding, oligomer formation, and amyloid fibril conversion.

Use Cases

• Modeling protein misfolding pathways based on atomic-resolution structural changes.
• Analyzing the role of electrostatic interactions in oligomer formation and fibril core topology.
• Studying the cytotoxic effects of soluble oligomers on cardiomyocytes prior to amyloid formation.
• Comparing aggregation kinetics between mutated patient-derived proteins and germline sequences.
• Investigating the structural strain introduced by mutations in complementary determining regions.

Strengths

• Data provides atomic-resolution tracking of protein misfolding steps, a first for this system according to the description.
• Includes comparative analysis of three protein variants: patient-derived FOR005, its single-point mutant FOR005-R49G, and the germline protein GL.

Limitations

• Column-level documentation is absent; field semantics must be inferred after download.
• Row count is unknown, which may limit suitability assessment.
• Last update date is unknown; freshness unverified.

Provenance

Source

paperswithcode

Collection Method

Experimental data from solution-state NMR spectroscopy.