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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...

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Genome-wide Protein-protein Interaction Screening by Protein-fragment Complementation Assay PCA in Living Cells

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Protein-protein interactions in a crowded environment.

Apratim Bhattacharya¹, Young C Kim², Jeetain Mittal³

¹Department of Chemical Engineering, Lehigh University, Bethlehem, PA, USA.

Biophysical Reviews

|May 17, 2017

Summary

Macromolecular crowding affects protein interactions within cells. New theories show that weak attractive forces between crowding molecules and proteins can unexpectedly destabilize protein complexes.

Keywords:

Cellular environment Crowding theories Dilute solution Macromolecular crowding Protein–crowder interactions Protein–protein interactions

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Area of Science:

Biochemistry
Molecular Biology
Cell Biology

Background:

Protein-protein interactions are vital for cellular functions like transcription and signal transduction.
Cellular environments are crowded with macromolecules, leading to non-specific interactions.
Traditional theories often assume crowding stabilizes protein associations through excluded volume effects.

Purpose of the Study:

To review recent advancements in understanding macromolecular crowding's impact on protein-protein interactions.
To present a developed crowding theory that quantitatively predicts binding free energy changes.
To explore the consequences of both repulsive and attractive protein-crowder interactions.

Main Methods:

Literature review of recent developments in macromolecular crowding research.
Theoretical modeling of protein-protein interactions under crowded conditions.
Quantitative prediction of binding free energy alterations due to crowding.

Main Results:

Crowding theory now quantitatively predicts binding free energy changes from protein-crowder interactions.
Weak attractive interactions between crowders and proteins can destabilize protein complex formation.
This finding contrasts with traditional theories solely based on entropic effects.

Conclusions:

Macromolecular crowding significantly influences protein-protein interactions beyond simple excluded volume effects.
Attractive crowder-protein interactions can disrupt protein complex stability, contrary to common assumptions.
Understanding these effects is crucial for comprehending cellular processes and protein complex dynamics.