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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...

Proteomics

Proteomics

A proteome is the entire set of proteins that a cell type produces. We can study proteomes using the knowledge of genomes because genes code for mRNAs, and the mRNAs encode proteins. Although mRNA analysis is a step in the right direction, not all mRNAs are translated into proteins.
Proteomics is the study of proteomes' function. It involves the large-scale systematic study of the proteome to denote the protein complement expressed by a genome. Scientist Mark Wilkins coined the term proteomics...

Conservation of Protein Domains

Conservation of Protein Domains

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...

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

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...

Structural Protein Function

Structural Protein Function

Structural proteins are a category of proteins responsible for functions ranging from cell shape and movement to providing support to major structures such as bones, cartilage, hair, and muscles. This group includes proteins such as collagen, actin, myosin, and keratin.
Collagen, the most abundant protein in mammals, is found throughout the body. In connective tissue, such as skin, ligaments, and tendons, it provides tensile strength and elasticity. In bones and teeth, it mineralizes to form...

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Related Experiment Video

Updated: Jun 3, 2026

JUMPn: A Streamlined Application for Protein Co-Expression Clustering and Network Analysis in Proteomics

JUMPn: A Streamlined Application for Protein Co-Expression Clustering and Network Analysis in Proteomics

Published on: October 19, 2021

Multi-scale sequence correlations increase proteome structural disorder and promiscuity.

Ariel Afek¹, Eugene I Shakhnovich, David B Lukatsky

¹Department of Chemistry, Ben-Gurion University of the Negev, Beer-Sheva, Israel.

Journal of Molecular Biology

|April 6, 2011

Summary

This summary is machine-generated.

Protein sequence correlations influence promiscuity and structural disorder. Enhanced sequence order in disordered proteins and proteomic hubs offers insights into protein interactions and aggregation diseases.

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Area of Science:

Biochemistry and Molecular Biology
Structural Biology
Systems Biology

Background:

Organismal proteomes exhibit significant protein promiscuity and structural disorder.
Understanding the drivers of nonspecific protein interactions and disordered structures is crucial.

Purpose of the Study:

To identify sequence-based factors contributing to protein promiscuity and structural disorder.
To investigate the role of multi-scale amino acid correlations in protein binding propensities.

Main Methods:

Statistical analysis of amino acid sequence correlations in proteomic datasets.
Development of an analytical theory to model sequence order effects.
Comparison of sequence properties between structurally ordered and disordered proteins.

Main Results:

Multi-scale sequence correlations statistically enhance intra- and inter-protein binding.
Structurally disordered proteins and proteomic hubs show enhanced sequence correlations.
Disordered proteins exhibit higher sequence order than ordered proteins.

Conclusions:

Sequence correlations are key determinants of protein promiscuity and disorder.
Findings provide a theoretical framework for understanding protein interactions.
Implications for molecular mechanisms underlying protein aggregation diseases.