TRPV1 Channel Conformational Dynamics via Encoded Coumarin Fluorescence

This dataset reports conformational dynamics in TRPV1 ion channels using the genetically encoded fluorescent amino acid coumarin-tyrosine at residue Y671. Data includes photon counts and optical fluctuations from coumarin within TRPV1 tetramers, correlating with channel activation by capsaicin. The findings are supported by molecular dynamics simulations showing solvent exposure changes at Y671.

Use Cases

• Analyze photon count data from coumarin fluorescence to correlate with TRPV1 channel activation states.
• Use optical fluctuation measurements as an optical marker for conformational dynamics at the selectivity filter.
• Cross-reference fluorescence data with molecular dynamics simulation results on Y671 solvent exposure.
• Investigate the relationship between capsaicin application and the reported coumarin signal for gating studies.

Strengths

• Data is derived from live-cell imaging via total internal reflection fluorescence microscopy.
• Findings are validated by complementary molecular dynamics simulations.
• Dataset is openly available under a CC0 1.0 license.

Limitations

• The specific data structure, column definitions, and sample size are not provided.
• Data is specialized for a specific biological system (TRPV1 channels) and experimental method.
• The dataset was last updated in January 2021 and may not reflect the most recent research.

Provenance

Source

Dryad digital repository.

Collection Method

Total internal reflection fluorescence microscopy on live cells and molecular dynamics simulations.

Freshness

Last updated on 2021-01-28.