ArticlePLoS computational biology2012
Structure and age jointly influence rates of protein evolution.
Article in PLoS computational biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
11 citing papers in PubMed, 23 citations in OpenAlex.
- Article
- Hypothesis: protein and RNA attributes are continuously optimized over time.BMC genomics · 2019Article
- The causes of evolvability and their evolution.Nature reviews. Genetics · 2019Review
- Metabolic Determinants of Enzyme Evolution in a Genome-Scale Bacterial Metabolic Network.Genome biology and evolution · 2018Article
- Correlates of evolutionary rates in the murine sperm proteome.BMC evolutionary biology · 2018Article
- New Genes and Functional Innovation in Mammals.Genome biology and evolution · 2017Article
- The Role of Evolutionary Selection in the Dynamics of Protein Structure Evolution.Biophysical journal · 2017Article
- Positive Selection Linked with Generation of Novel Mammalian Dentition Patterns.Genome biology and evolution · 2016Article
- Article
- Exploring fold space preferences of new-born and ancient protein superfamilies.PLoS computational biology · 2013Article
- Linking molecular evolution to molecular grafting.The Journal of biological chemistryReview
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
Abstract
What factors determine a protein's rate of evolution are actively debated. Especially unclear is the relative role of intrinsic factors of present-day proteins versus historical factors such as protein age. Here we study the interplay of structural properties and evolutionary age, as determinants of protein evolutionary rate. We use a large set of one-to-one orthologs between human and mouse proteins, with mapped PDB structures. We report that previously observed structural correlations also hold within each age group - including relationships between solvent accessibility, designabililty, and evolutionary rates. However, age also plays a crucial role: age modulates the relationship between solvent accessibility and rate. Additionally, younger proteins, despite being less designable, tend to evolve faster than older proteins. We show that previously reported relationships between age and rate cannot be explained by structural biases among age groups. Finally, we introduce a knowledge-based potential function to study the stability of proteins through large-scale computation. We find that older proteins are more stable for their native structure, and more robust to mutations, than younger ones. Our results underscore that several determinants, both intrinsic and historical, can interact to determine rates of protein evolution.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.