Bound Water at Protein-Protein Interfaces: Partners, Roles and Hydrophobic Bubbles as a Conserved Motif
2011

Understanding Water's Role in Protein-Protein Interactions

Sample size: 179 publication Evidence: moderate

Author Information

Author(s): Ahmed Mostafa H., Spyrakis Francesca, Cozzini Pietro, Tripathi Parijat K., Mozzarelli Andrea, Scarsdale J. Neel, Safo Martin A., Kellogg Glen E.

Primary Institution: Virginia Commonwealth University

Hypothesis

What roles do water molecules play at protein-protein interfaces?

Conclusion

Water molecules at protein-protein interfaces can stabilize interactions, but many do not contribute favorably to the interaction energy.

Supporting Evidence

  • 21% of water molecules at interfaces are involved in bridging interactions.
  • 53% interact with only one protein, while 26% show no significant interactions.
  • 42% of non-interacting waters are buried in hydrophobic environments.

Takeaway

Water helps proteins stick together, but sometimes it just gets in the way and doesn't help at all.

Methodology

Analyzed 4741 water molecules from 179 high-resolution X-ray crystal structures of protein-protein complexes using modeling tools.

Limitations

The study is based on crystallographic data, which may not fully represent dynamic biological conditions.

Digital Object Identifier (DOI)

10.1371/journal.pone.0024712

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