Three-Dimensional Structures of Membrane Proteins from Genomic Sequencing

@article{Hopf2012ThreeDimensionalSO,
  title={Three-Dimensional Structures of Membrane Proteins from Genomic Sequencing},
  author={Thomas A. Hopf and Lucy J. Colwell and Robert Sheridan and Burkhard Rost and Chris Sander and Debora S. Marks},
  journal={Cell},
  year={2012},
  volume={149},
  pages={1607-1621}
}
We show that amino acid covariation in proteins, extracted from the evolutionary sequence record, can be used to fold transmembrane proteins. We use this technique to predict previously unknown 3D structures for 11 transmembrane proteins (with up to 14 helices) from their sequences alone. The prediction method (EVfold_membrane) applies a maximum entropy approach to infer evolutionary covariation in pairs of sequence positions within a protein family and then generates all-atom models with the… CONTINUE READING
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