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Force Spectroscopy of Single Protein Molecules Using an Atomic Force Microscope
Published on: February 28, 2019
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Seeing and sensing single G protein-coupled receptors by atomic force microscopy
K Tanuj Sapra1, Patrizia M Spoerri1, Andreas Engel1
1ETH Zürich, Department of Biosystems Science and Engineering, Mattenstrasse 26, 4058 Basel, Switzerland.
Current Opinion in Cell Biology
|November 10, 2018
Summary
Atomic force microscopy (AFM) reveals the dynamic conformations of G protein-coupled receptors (GPCRs). This technique quantifies ligand binding and structural changes, offering new insights into GPCR function.
Area of Science:
- Biophysics
- Cell Biology
- Structural Biology
Background:
- G protein-coupled receptors (GPCRs) are crucial cell membrane proteins that transduce extracellular signals.
- GPCRs exist in a dynamic range of conformations, often not fully represented in static structural data.
- Understanding these dynamic states is essential for elucidating GPCR function.
Purpose of the Study:
- To explore the utility of Atomic Force Microscopy (AFM) for investigating GPCRs.
- To quantify the physical and chemical properties of dynamic GPCR conformations.
- To observe GPCR supramolecular assembly and ligand-binding interactions in native environments.
Main Methods:
- High-resolution imaging and force spectroscopy using AFM.
- Direct observation of GPCRs within native cell membranes.
- Measurement of ligand-binding free-energy landscapes and interaction-induced structural modulations.
Main Results:
- AFM successfully visualized GPCR supramolecular assembly in native membranes.
- The study quantified ligand-binding free-energy landscapes for GPCRs.
- AFM revealed how molecular interactions modulate GPCR structural properties.
Conclusions:
- AFM provides unique insights into the dynamic nature and function of GPCRs.
- Emerging trends in GPCR function are becoming apparent through AFM studies.
- Future integration of AFM with superresolution fluorescence imaging promises deeper understanding of GPCRs in cellular contexts.
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