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Protein-protein Interfaces

Protein-protein Interfaces

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...

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Updated: Sep 27, 2025

Real Time Measurements of Membrane Protein:Receptor Interactions Using Surface Plasmon Resonance SPR

Real Time Measurements of Membrane Protein:Receptor Interactions Using Surface Plasmon Resonance SPR

Published on: November 29, 2014

Multivalent Interactions with Intrinsically Disordered Proteins Probed by Surface Plasmon Resonance.

Larisa E Kapinos¹, Roderick Y H Lim²

¹Biozentrum and the Swiss Nanoscience Institute, University of Basel Switzerland, Basel, Switzerland.

Methods in Molecular Biology (Clifton, N.J.)

|April 12, 2022

Summary

This study quantifies the multivalent interactions between nuclear transport receptors (NTRs) and phenylalanine-glycine nucleoporins (FG Nups) using surface plasmon resonance (SPR). The findings reveal how these interactions influence nucleocytoplasmic transport (NCT) and protein binding dynamics.

Keywords:

Biological interface Exportin FG Nucleoporins Importin Intrinsically disordered proteins Karyopherin Multivalent interactions Nuclear pore complex Steady state Surface plasmon resonance

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Area of Science:

Biochemistry and Molecular Biology
Cell Biology
Biophysics

Background:

Multivalent interactions are crucial for protein associations, particularly in regulating nucleocytoplasmic transport (NCT) by nuclear transport receptors (NTRs) and intrinsically disordered proteins (IDPs).
Phenylalanine-glycine nucleoporins (FG Nups), a class of IDPs, mediate selective and rapid transport through the nuclear pore complex (NPC) via multivalent interactions with NTRs.

Purpose of the Study:

To quantify the binding affinity and kinetics of NTR-FG Nup interactions using surface plasmon resonance (SPR).
To investigate the impact of FG Nup surface density on these multivalent interactions.
To develop and describe an in situ method for measuring conformational changes in FG Nup layers upon NTR binding.

Main Methods:

Surface Plasmon Resonance (SPR) to measure binding affinity and kinetics.
In situ conformational height change measurements.
Analysis of SPR data considering mass transport limitations.

Main Results:

Quantitative data on NTR-FG Nup binding affinity and kinetics as a function of FG Nup surface density.
Demonstration of an SPR-based method to detect conformational changes in FG Nup layers upon NTR binding.
Established protocols for analyzing SPR data, accounting for mass transport effects.

Conclusions:

SPR is a valuable tool for studying multivalent interactions and avidity in biological systems.
The methodology provides insights into the mechanisms of nucleocytoplasmic transport and FG Nup-NTR interactions.
This approach can be broadly applied to diverse biointerfacial systems involving multivalent binding.