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Comment
. 2019 Jul 12;365(6449):120-121.
doi: 10.1126/science.aay1440.

Mapping global protein contacts

Sandor Vajda  1 , Andrew Emili  2
Affiliations
Comment

Mapping global protein contacts

Sandor Vajda et al. Science. .
No abstract available

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Figures

Figure 1.
Figure 1.. From protein pairs to complex interaction networks
With the method shown below, co-evolutionary analyses of amino-acid contacts in E. coli protein pairs can unearth new interprotein contacts that serve to expand protein interaction networks and illuminate fresh functional relationships. The multiple sequence alignment shown in the "Analyze" step is for a hypothetical E. coli protein (blue rectangles) and its orthologs (gray rectangles). Red boxes indicate interprotein contacts predicted by GREMLIN.
See this image and copyright information in PMC

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References

    1. Marks DS, Hopf TA, Sander C, Protein structure prediction from sequence variation. Nat Biotechnol 30, 1072–1080 (2012). - PMC - PubMed
    1. R. F. Service, Google’s DeepMind aces protein folding. Science, (2018).
    1. Lichtarge O, Bourne HR, Cohen FE, An evolutionary trace method defines binding surfaces common to protein families. Journal of molecular biology 257, 342–358 (1996). - PubMed
    1. Ovchinnikov S, Kamisetty H, Baker D, Robust and accurate prediction of residue-residue interactions across protein interfaces using evolutionary information. Elife 3, (2014). - PMC - PubMed
    1. Schwikowski B, Uetz P, Fields S, A network of protein-protein interactions in yeast. Nat Biotechnol 18, 1257–1261 (2000). - PubMed

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