ArticleScientific reports2015
On the origin of protein superfamilies and superfolds.
Article in Scientific reports, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 22 citations in OpenAlex.
- Protein superfolds are characterised as frustration-free topologies: A case study of pure parallel β-sheet topologies.PLoS computational biology · 2024Article
- ICARUS: flexible protein structural alignment based on Protein Units.Bioinformatics (Oxford, England) · 2023Article
- Engineering functional thermostable proteins using ancestral sequence reconstruction.The Journal of biological chemistry · 2022Review
- A Method for Assessing the Robustness of Protein Structures by Randomizing Packing Interactions.Frontiers in molecular biosciences · 2022Article
- A global map of the protein shape universe.PLoS computational biology · 2019Article
- Article
- A Study of the Boltzmann Sequence-Structure Channel.Proceedings of the IEEE. Institute of Electrical and Electronics Engineers · 2017Article
- A Dynamic Model for the Evolution of Protein Structure.Journal of molecular evolution · 2016Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Distributions of protein families and folds in genomes are highly skewed, having a small number of prevalent superfamiles/superfolds and a large number of families/folds of a small size. Why are the distributions of protein families and folds skewed? Why are there only a limited number of protein families? Here, we employ an information theoretic approach to investigate the protein sequence-structure relationship that leads to the skewed distributions. We consider that protein sequences and folds constitute an information theoretic channel and computed the most efficient distribution of sequences that code all protein folds. The identified distributions of sequences and folds are found to follow a power law, consistent with those observed for proteins in nature. Importantly, the skewed distributions of sequences and folds are suggested to have different origins: the skewed distribution of sequences is due to evolutionary pressure to achieve efficient coding of necessary folds, whereas that of folds is based on the thermodynamic stability of folds. The current study provides a new information theoretic framework for proteins that could be widely applied for understanding protein sequences, structures, functions, and interactions.
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