Transmembrane Protein 3D Structures - Predicted by Evolutionary Couplings

New EVfold Predications for α-Helical Transmembrane Proteins

This page links you to our most recent EVfold runs for α-helical membrane proteins (EVfold - Membrane 2.0). This includes updated results from all the proteins that were presented in our 2012 paper ( Hopf et al 2012 ). We recommend you use these rather than the older results as we can see that where a comparison can be made to a known crystal structure (our benchmark set), all evolutionary couplings (ECs) are more accurate with respect to real contacts and all predicted 3D structures are more accurate compared to the crystals. This is due to the use of the improved algorithm and the increase in the number of sequences available.

---We will be updating these results regularly.


This site will be updated regularly to include all α-helical transmembrane protein families that have sufficient diverse sequences.

Comparison to known structures:

Evolutionary couplings and predicted 3D folds for membrane proteins compared to known 3D structures.

Predictions for unknown structures:

Evolutionary couplings and predicted 3D folds for proteins that have unknown structures, either for the specific protein or any other family member. The high ranked EC residue pairs may also be informative of functional sites.