Related Experiment Video
Updated: May 15, 2026

10:37
Deep Proteome Profiling by Isobaric Labeling, Extensive Liquid Chromatography, Mass Spectrometry, and Software-assisted Quantification
Published on: November 15, 2017
Exploring charged biased regions in the human proteome.
1Molecular and Cellular Diagnosis Processes, Centre of Biotechnology of Sfax, University of Sfax, Route Sidi Mansour, Po Box 1177, 3018 Sfax, Tunisia.
Gene
|December 26, 2012
Summary
Charged regions in human proteins are linked to crucial roles, including DNA binding and regulation. This study identified 446 charged biased proteins, highlighting their functional significance in the human proteome.
Area of Science:
- Proteomics
- Bioinformatics
- Genomics
Background:
- Biased regions in proteins are increasingly recognized for their structural and functional importance.
- These regions are often associated with protein disorder or specific cellular roles.
Purpose of the Study:
- To investigate charged biased protein sequences within the human genome.
- To identify and characterize the functions associated with these charged regions.
Main Methods:
- Analysis of the human proteome to identify charged biased protein sequences.
- Utilized Gene Ontology analysis to determine the functions of identified proteins.
Main Results:
- Identified 446 charged biased proteins in the human proteome.
- Negative charge runs are prevalent in transcription factors, importins, and protein kinases.
- Positive charge clusters are significantly associated with ribosomal proteins.
- Proteins with zinc-binding fingers often exhibit mixed charged regions.
- Gene Ontology analysis indicates charged proteins are primarily involved in regulatory functions.
Conclusions:
- Charged biased regions are critical determinants of protein function in humans.
- These regions play key roles in DNA binding, protein transport, and cellular regulation.
- The distribution and characteristics of charged regions provide insights into protein evolution and function.
Related Concept Videos
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...
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...
Protein Networks
An organism can have thousands of different proteins, and these proteins must cooperate to ensure the health of an organism. Proteins bind to other proteins and form complexes to carry out their functions. Many proteins interact with multiple other proteins creating a complex network of protein interactions.
These interactions can be represented through maps depicting protein-protein interaction networks, represented as nodes and edges. Nodes are circles that are representative of a protein,...
These interactions can be represented through maps depicting protein-protein interaction networks, represented as nodes and edges. Nodes are circles that are representative of a protein,...
Western Blotting
Western blotting is an analytical technique for protein identification. It has various applications in immunology and medicine, including detecting diseases like bovine spongiform encephalopathy, mad cow disease, and human and feline immunodeficiency virus from biological samples.
The technique begins with separating proteins from the sample using sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), followed by protein transfer, immunoblotting, and finally, protein detection.
The technique begins with separating proteins from the sample using sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), followed by protein transfer, immunoblotting, and finally, protein detection.
