MemMoRF

MemMoRF catalogs disordered protein regions that interact with cellular membranes (Membrane-associated Molecular Recognition Features, MemMoRFs) and associates experimentally validated entries with NMR-derived secondary structure propensity and flexibility data.

Key Features:

• Experimental validation: Entries are supported by experimental evidence compiled from the literature and structural data.
• Manual curation: Records are assembled through meticulous manual curation of existing scientific publications and structural datasets.
• NMR-derived structural information: Secondary structure propensity and flexibility information are derived from nuclear magnetic resonance (NMR) chemical shifts.
• Contextual annotations: Functional annotations and disease-related insights are extracted directly from scientific papers.
• Disorder-to-order characterization: Documentation includes disorder-to-order transitions of intrinsically disordered protein regions (IDRs) upon lipid interaction, analogous to Molecular Recognition Features (MoRFs).
• Biological process linkage: Associations to processes such as signaling, vesicle trafficking, and viral invasion are recorded.

Scientific Applications:

• Signaling studies: Investigating roles of membrane-interacting IDRs in cellular signaling pathways.
• Vesicle trafficking research: Analyzing involvement of MemMoRFs in vesicle formation and trafficking.
• Viral invasion mechanisms: Studying membrane-associated IDRs implicated in viral entry and membrane interactions.
• Protein–membrane dynamics: Characterizing disorder-to-order transitions and lipid interaction mechanisms of IDRs.
• Disease association analysis: Exploring disease-related implications of membrane-associated disordered regions.

Methodology:

Entries were compiled by manual curation of literature and structural data; secondary structure propensity and flexibility were derived from NMR chemical shifts; contextual functional and disease annotations were extracted from scientific papers.