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Conservation of Protein Domains

Conservation of Protein Domains

Conservation of Protein Domains Over Different Proteins

Conservation of Protein Domains Over Different Proteins

Protein domains are small structurally independent units that are part of a single amino acid chain. Although these domains are often structurally independent, they may rely on synergistic effects to perform their functions as part of a larger protein. Protein domains may be conserved within the same organism, as well as across different organisms.
A limited set of protein domains often duplicate and recombine during evolution. These domains can be organized in different combinations to...

Conserved Binding Sites

Conserved Binding Sites

Many proteins’ biological role depends on their interactions with their ligands, small molecules that bind to specific locations on the protein known as ligand-binding sites. Ligand-binding sites are often conserved among homologous proteins as these sites are critical for protein function.
Binding sites are often located in large pockets, and if their location on a protein’s surface is unknown, it can be predicted using various approaches. The energetic method computationally...

Conserved Binding Sites

Conserved Binding Sites

Intrinsically Disordered Proteins

Intrinsically Disordered Proteins

Intrinsically disordered proteins are a group of proteins that do not fold into specific three-dimensional structures. Their structural flexibility allows them to complement ordered proteins to perform functions that are inaccessible to rigid structures. They are more common in eukaryotes than prokaryotes and may either be exclusively intrinsically disordered or hybrid proteins, consisting of a mix of ordered and disordered regions. The absence of a rigid structure in these proteins can be...

Intrinsically Disordered Proteins

Intrinsically Disordered Proteins

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Related Experiment Video

Updated: May 6, 2026

Quantifying Tissue-Specific Proteostatic Decline in Caenorhabditis elegans

Quantifying Tissue-Specific Proteostatic Decline in Caenorhabditis elegans

Published on: September 7, 2021

Conserved proteins are fragile.

Raquel Assis¹, Alexey S Kondrashov

¹Department of Biology, Pennsylvania State University.

Molecular Biology and Evolution

|November 9, 2013

Summary

This summary is machine-generated.

Slowly evolving proteins are fragile, not just essential. Fragility, measured by missense mutation impact, better predicts evolutionary rate than essentiality, highlighting protein network interdependence.

Keywords:

evolutionary rate natural selection protein essentiality protein evolution selective constraint

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Last Updated: May 6, 2026

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Coupled Assays for Monitoring Protein Refolding in Saccharomyces cerevisiae

Coupled Assays for Monitoring Protein Refolding in Saccharomyces cerevisiae

Published on: July 9, 2013

Area of Science:

Evolutionary biology
Molecular biology
Genomics

Background:

Selective constraint on proteins varies, often linked to functional importance.
Protein evolutionary rates can also be limited by fragility, where mutations decrease fitness.

Purpose of the Study:

To differentiate the roles of essentiality and fragility in selective constraint.
To compare the predictive power of selection against nonsense mutations (snon) and missense mutations (smis) for protein sequence conservation (Ka).

Main Methods:

Compared snon and smis to Ka across proteins.
Assessed correlations between snon/smis and gene expression, tissue specificity, and protein-protein interactions.

Main Results:

Selection against missense mutations (smis) showed a stronger correlation with protein sequence conservation (Ka) than selection against nonsense mutations (snon).
smis was more strongly correlated with gene expression, tissue specificity, and protein interactions than snon.

Conclusions:

Protein fragility, indicated by sensitivity to missense mutations, is a primary driver of strong selective constraint.
This fragility's impact on biological networks suggests functional impairment is more detrimental than complete loss.