Structure of a functional amyloid protein subunit computed using sequence variation.

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Large-scale determination of previously unsolved protein structures using evolutionary information (2015, methodology): “…from such predictions have been used to model a wide range of unknown protein structures ( Hayat et al., 2014 ; Wickles et al., 2014 ; Abriata, 2015 ; Antala et al., 2015 ; Hopf et al., 2015 ; Tian et al., 2015 ) and protein–protein complexes ( Ovchinnikov et al., 2014 ; Hopf et al., 2014 ).”
Structure of the Bacterial Cytoskeleton Protein Bactofilin by NMR Chemical Shifts and Sequence Variation. (2016, methodology): “We recently described an approach to determine structures of naturally occurring fibrillar proteins using amino acid contacts derived from an analysis of multiple sequence alignments (MSAs) (14).”
Structured states of disordered proteins from genomic sequences (2016, unknown): “local ECs are consistent with previously proposed amyloid organization (Figures S6) (Tian et al., 2015).”
Large-scale identification of coevolution signals across homo-oligomeric protein interfaces by direct coupling analysis (2017, background): “In the context of tertiary-structure prediction of proteins, this has been tested across hundreds of protein families, and in turn has led to a large number of in-silico tertiary-structure models (10-13) for a large variety of protein families, each one containing thousands of proteins but not havin”