Search research articles

ABOUT JoVE

Overview Leadership Blog JoVE Help Center

AUTHORS

Publishing Process Editorial Board Scope & Policies Peer Review FAQ Submit

LIBRARIANS

Testimonials Subscriptions Access Resources Library Advisory Board FAQ

RESEARCH

JoVE Journal Methods Collections JoVE Encyclopedia of Experiments Archive

EDUCATION

JoVE Core JoVE Business JoVE Science Education JoVE Lab Manual Faculty Resource Center Faculty Site

Terms & Conditions of Use

Related Concept Videos

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 analyses the...

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 analyses the...

Protein Families

Protein Families

Protein families are groups of homologous proteins; that is, they have similarities in amino acid sequences and three-dimensional structures. Protein families usually occur because of gene duplication, where an additional copy of a gene is inserted into the genome of an organism. Mutations that change the amino acids but still allow the protein to be properly synthesized, will lead to new protein family members. If these new proteins contain similar amino acids in key locations, protein...

Protein Families

Protein Families

Protein families are groups of homologous proteins; that is, they have similarities in amino acid sequences and three-dimensional structures. Protein families usually occur because of gene duplication, where an additional copy of a gene is inserted into the genome of an organism. Mutations that change the amino acids but still allow the protein to be properly synthesized, will lead to new protein family members. If these new proteins contain similar amino acids in key locations, protein...

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 form...

Multi-species Conserved Sequences

Multi-species Conserved Sequences

Next-generation sequencing technologies have created large genomic databases of a variety of animals and plants. Ever since the human genome project was completed, scientists studied the genome of primates, mammals, and other phylogenetically distant living beings. Such large-scale studies have provided new insights into the evolutionary relationship between organisms.
Although the genome of each species varies greatly from each other, a few sequences are highly conserved. Such conserved DNA...

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by

Same author

Linking protein aggregation and structural stability to predict pathogenic MYH7 variants via machine learning.

Journal of structural biology·2026

Same author

Protein tandem repeats that produce frameshifts can generate new structural states and functions.

The FEBS journal·2025

Same author

Engineering of a Complex of the DNase Domain of Colicin E9 with the Immunity Protein Im9 Activated by the Protease pS273R of African Swine Fever Virus.

ACS synthetic biology·2025

Same author

When artificial intelligence meets protein research.

Open research Europe·2025

Same author

Application of artificial intelligence for the prediction of amyloidoses.

Neural regeneration research·2025

Same author

Cross-reactivity of rPvs48/45, a recombinant Plasmodium vivax protein, with plasma from Plasmodium falciparum endemic areas of Africa.

PloS one·2025

Same journal

Transcriptomic insights into epigenetic and immunomodulatory roles of nuclear histone genes in bladder cancer: A bioinformatics approach.

Advances in protein chemistry and structural biology·2026

Same journal

Investigating the immune-modulatory association of miRNAs in HPV-associated HNSCC individuals: A bioinformatics approach.

Advances in protein chemistry and structural biology·2026

Same journal

VISTA as a Double-Edged immune checkpoint molecule in cancer and autoimmunity.

Advances in protein chemistry and structural biology·2026

Same journal

Aptamers as immunomodulatory therapeutic alternatives targeting neglected tropical diseases (NTDs).

Advances in protein chemistry and structural biology·2026

Same journal

Peptides and peptidomimetics as immunomodulator agents targeting neglected tropical diseases.

Advances in protein chemistry and structural biology·2026

Same journal

Transcriptomic profiling reveals immune pathway dysregulation and key interferon-responsive genes in Systemic Lupus Erythematosus.

Advances in protein chemistry and structural biology·2026

See all related articles

Search research articles

Related Experiment Video

Updated: Jun 11, 2026

Computational Prediction of Amino Acid Preferences of Potentially Multispecific Peptide-Binding Domains Involved in Protein-Protein Interactions

Computational Prediction of Amino Acid Preferences of Potentially Multispecific Peptide-Binding Domains Involved in Protein-Protein Interactions

Published on: January 26, 2024

Protein homorepeats sequences, structures, evolution, and functions.

Julien Jorda¹, Andrey V Kajava

¹Centre de Recherches de Biochimie Macromoléculaire UMR 5237, CNRS, University of Montpellier 1 and 2, Montpellier, France.

Advances in Protein Chemistry and Structural Biology

|July 13, 2010

Summary

This summary is machine-generated.

Homorepeats, or single amino acid runs, are rare but important protein motifs. These sequences influence protein structure, function, and are linked to diseases.

More Related Videos

Identification of Functional Protein Regions Through Chimeric Protein Construction

Identification of Functional Protein Regions Through Chimeric Protein Construction

Published on: January 8, 2019

Optimization of Synthetic Proteins: Identification of Interpositional Dependencies Indicating Structurally and/or Functionally Linked Residues

Optimization of Synthetic Proteins: Identification of Interpositional Dependencies Indicating Structurally and/or Functionally Linked Residues

Published on: July 14, 2015

Related Experiment Videos

Last Updated: Jun 11, 2026

Computational Prediction of Amino Acid Preferences of Potentially Multispecific Peptide-Binding Domains Involved in Protein-Protein Interactions

Computational Prediction of Amino Acid Preferences of Potentially Multispecific Peptide-Binding Domains Involved in Protein-Protein Interactions

Published on: January 26, 2024

Identification of Functional Protein Regions Through Chimeric Protein Construction

Identification of Functional Protein Regions Through Chimeric Protein Construction

Published on: January 8, 2019

Optimization of Synthetic Proteins: Identification of Interpositional Dependencies Indicating Structurally and/or Functionally Linked Residues

Optimization of Synthetic Proteins: Identification of Interpositional Dependencies Indicating Structurally and/or Functionally Linked Residues

Published on: July 14, 2015

Area of Science:

Proteomics
Structural Biology
Biochemistry

Background:

Most protein sequences are aperiodic, utilizing a mix of amino acids.
Homorepeats, defined as runs of a single amino acid residue, are uncommon yet significant motifs.
These runs possess unique physico-chemical properties due to high local amino acid concentration.

Purpose of the Study:

To review the distribution and characteristics of homorepeats in proteomes.
To explore the structural properties, evolutionary significance, and functional roles of homorepeats.
To highlight the association of homorepeats with hereditary and age-related diseases.

Main Methods:

Bioinformatic analysis of proteome data.
Comparative sequence analysis.
Literature review of existing studies on homorepeats.

Main Results:

Homorepeats are found across various proteomes, exhibiting distinct distribution patterns.
These motifs contribute novel structural and functional attributes to proteins.
Homorepeat presence is correlated with specific biological processes and disease states.

Conclusions:

Homorepeats are crucial elements in protein architecture and function.
Understanding homorepeat biology is vital for insights into health and disease.
Further research into homorepeats promises advancements in molecular biology and medicine.