Inter-residue, inter-protein and inter-family coevolution: bridging the scales
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Interacting proteins coevolve at multiple but interconnected scales, from the residue-residue over the protein-protein up to the family-family level. The recent accumulation of enormous amounts of sequence data allows for the development of novel, data-driven computational approaches. Notably, these approaches can bridge scales within a single statistical framework. Although being currently applied mostly to isolated problems on single scales, their immense potential for an evolutionary informed, structural systems biology is steadily emerging.
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More recent methods incorporate inter-protein residue-residue contact predictions obtained via co-evolutionary analysis and a deep learning algorithm.
“More recent methods incorporate inter-protein residue-residue contact predictions obtained via co-evolutionary analysis17 and a deep learning algorithm18.”
From AF2Complex predicts direct physical interactions in multimeric proteins with deep learning (2022) · cites this paper as [17]
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- Authors
- Szurmant, H., & Weigt, M.
- Affiliations
- Western University of Health Sciences (US)
- Centre National de la Recherche Scientifique (FR)
- Corresponding author
- Szurmant, Hendrik
- Weigt, Martin
- Venue
- Current Opinion in Structural Biology
- Publisher
- Elsevier BV
- Published
- 2018-06
- Volume
- 50
- Pages
- 26-32
- ISSN
- 0959-440X (ISSN-L)
- PMC
- PMC5940578
- OpenAlex
- W2766246727
- Cited by
- 81
- References
- 53
- Citations by year
- 2026: 4 · 2025: 1 · 2024: 7 · 2023: 8 · 2022: 13 · 2021: 12 · 2020: 10 · 2019: 22 · 2018: 4
- FWCI
- 0.92
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Current Opinion in Structural Biology (acceptedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- arXiv (Cornell University) (submittedVersion)
- HAL (submittedVersion)
- arXiv (Cornell University)
- Funders
- Horizon 2020 (GM106085, 734439)
- National Institute of General Medical Sciences
- Agence Nationale de la Recherche (ANR-13-BS04-0012-01)
- National Institutes of Health
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Phylogenetic Studies
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Evolution and Genetic Dynamics
- Keywords
- coevolution, protein-protein interaction, residue-residue interactions, protein families, protein sequence evolution
- MeSH terms
- Amino Acid Sequence, Amino Acids, Binding Sites, Multigene Family, Models, Molecular, Protein Binding, Protein Conformation, Proteins, Evolution, Molecular, Quantitative Structure-Activity Relationship, Databases, Protein
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
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