Understanding Information Transfer in Protein Domains
Author Information
Author(s): Lenaerts Tom, Ferkinghoff-Borg Jesper, Stricher Francois, Serrano Luis, Schymkowitz Joost WH, Rousseau Frederic
Primary Institution: VIB, Brussels, Belgium
Hypothesis
Can protein dynamics be analyzed using information theory to quantify information exchange between functional sites?
Conclusion
The method developed allows for mapping biological information exchange on protein structures, revealing how binding triggers conformational changes.
Supporting Evidence
- The Fyn SH2 domain acts as a noisy communication channel linking distant residues.
- Mutual information quantifies the amount of conformational dependence between protein residues.
- The study identifies a network of residues that exchange information upon ligand binding.
Takeaway
This study shows how proteins communicate internally, like a game of telephone, where one part of the protein can send messages to another part, even if they are far apart.
Methodology
The study uses Monte Carlo dynamics simulations and information theory to analyze conformational correlations and quantify information exchange in the Fyn SH2 domain.
Limitations
The analysis assumes no large structural changes between bound and unbound states, which may not hold true for all proteins.
Digital Object Identifier (DOI)
Want to read the original?
Access the complete publication on the publisher's website