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Protein-protein Interfaces

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Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a polypeptide...

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Related Experiment Video

Updated: Jul 14, 2026

Proton Transfer and Protein Conformation Dynamics in Photosensitive Proteins by Time-resolved Step-scan Fourier-transform Infrared Spectroscopy

Proton Transfer and Protein Conformation Dynamics in Photosensitive Proteins by Time-resolved Step-scan Fourier-transform Infrared Spectroscopy

Published on: June 27, 2014

Electrostatic and steric interactions determine bacteriorhodopsin single-molecule biomechanics.

Kislon Voïtchovsky¹, Sonia Antoranz Contera, J F Ryan

¹Bionanotechnology Interdisciplinary Research Collaboration, Department of Physics, Clarendon Laboratory, University of Oxford, Oxford, United Kingdom.

Biophysical Journal

|May 22, 2007

Summary

Tryptophan residues in bacteriorhodopsin form a rigid scaffold, controlling protein mechanics and enabling proton pumping. This extracellular network is crucial for the efficiency of haloarchaeal rhodopsins.

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Bio-layer Interferometry for Measuring Kinetics of Protein-protein Interactions and Allosteric Ligand Effects

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Published on: February 18, 2014

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Last Updated: Jul 14, 2026

Proton Transfer and Protein Conformation Dynamics in Photosensitive Proteins by Time-resolved Step-scan Fourier-transform Infrared Spectroscopy

Proton Transfer and Protein Conformation Dynamics in Photosensitive Proteins by Time-resolved Step-scan Fourier-transform Infrared Spectroscopy

Published on: June 27, 2014

Bio-layer Interferometry for Measuring Kinetics of Protein-protein Interactions and Allosteric Ligand Effects

Bio-layer Interferometry for Measuring Kinetics of Protein-protein Interactions and Allosteric Ligand Effects

Published on: February 18, 2014

Area of Science:

Structural Biology
Biophysics
Membrane Protein Dynamics

Background:

Bacteriorhodopsin (bR) is a light-driven proton pump in haloarchaea.
Its function relies on photon energy conversion into structural changes for proton translocation.
Understanding bR biomechanics at the submolecular level is key to its efficient function.

Purpose of the Study:

To investigate the role of tryptophan (Trp) residues in bacteriorhodopsin's mechanical properties.
To elucidate how Trp residues contribute to the protein's scaffold and proton pumping mechanism.
To explore the influence of salt concentration on bR structure and function.

Main Methods:

Single molecule force spectroscopy was employed.
Experiments were conducted at varying salt concentrations.
Analysis focused on the mechanical contributions of specific amino acid residues.

Main Results:

Tryptophan residues form a rigid extracellular scaffold, creating major unfolding barriers.
This Trp-based network encloses the retinal, dictates local mechanical properties, and anchors bR.
Extracellular Trp residues facilitate ion binding for proton release and transport, while the cytoplasmic side offers flexibility.

Conclusions:

A stable, extracellular Trp-based network is critical for bacteriorhodopsin's mechanical stability and function.
This network controls proton translocation by anchoring the protein and facilitating ion binding.
The identified Trp network is likely conserved in other haloarchaeal rhodopsins, contributing to their high efficiency.