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Protein Dynamics in Living Cells

Protein Dynamics in Living Cells

Different fluorescence-based techniques are used to study the protein dynamics in living cells. These techniques include FRAP, FRET, and PET.
Fluorescent recovery after photobleaching (FRAP) is a fluorescent-protein-based detection technique used to quantify protein movement rates within the cell. This method exposes a small portion of the cell to an intense laser beam. The laser beam causes permanent photobleaching of the fluorophore-tagged proteins in the exposed region. As the bleached...

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Related Experiment Video

Updated: Jun 13, 2025

Yeast Luminometric and Xenopus Oocyte Electrophysiological Examinations of the Molecular Mechanosensitivity of TRPV4

Yeast Luminometric and Xenopus Oocyte Electrophysiological Examinations of the Molecular Mechanosensitivity of TRPV4

Published on: December 31, 2013

TRPM8 protein dynamics correlates with ligand structure and cellular function.

Mubark D Mebrat^1,2, Dustin D Luu^1,2, Jacob K Hilton^1,2

¹School of Molecular Sciences, Arizona State University, Tempe, AZ 85281, United States.

Biorxiv : the Preprint Server for Biology

|June 4, 2025

Summary

This summary is machine-generated.

Researchers linked human cold receptor TRPM8 protein dynamics, chemical structure, and cellular function. This finding offers a predictive bridge for drug discovery targeting TRPM8, potentially reducing side effects.

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Last Updated: Jun 13, 2025

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Purification and Reconstitution of TRPV1 for Spectroscopic Analysis

Purification and Reconstitution of TRPV1 for Spectroscopic Analysis

Published on: July 3, 2018

Area of Science:

Structural Biology
Computational Chemistry
Pharmacology

Background:

Protein dynamics are crucial for biological function.
The TRPM8 receptor is a target for pain relief but causes side effects.
Understanding TRPM8 dynamics is key to developing safer therapeutics.

Purpose of the Study:

To investigate the relationship between TRPM8 protein dynamics, chemical structure, and cellular potency.
To establish a predictive model linking chemical structure to protein dynamics and function.
To explore TRPM8 as a target for drug discovery with reduced side effects.

Main Methods:

Nuclear Magnetic Resonance (NMR) spectroscopy to study TRPM8 dynamics.
Computational cheminformatics analysis of small molecule ligands.
Electrophysiology to assess cellular function and compound potency.

Main Results:

Cheminformatic analysis correlated TRPM8 ligand library with cellular function.
Electrophysiology confirmed a link between chemical structure and compound potency.
NMR studies revealed ligand binding conformationally selects TRPM8 dynamics, correlating with chemical structure.

Conclusions:

Protein dynamics serve as a quantifiable link between chemical structure and cellular function for TRPM8.
This relationship can be used predictively in drug discovery.
Findings have implications for developing safer TRPM8-targeting drugs for pain indications.