Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

Two-dimensional Gel Electrophoresis01:22

Two-dimensional Gel Electrophoresis

6.6K
Two-dimensional gel electrophoresis is a high-resolution protein separation method first introduced by O' Farrell and Klose in 1975. This method involves protein separation by two dimensions, mass and charge, making it more accurate than one-dimensional gel electrophoresis.
The first dimension separation uses the isoelectric focusing or IEF technique performed on immobilized pH gradient (IPG) strips that separate proteins according to their isoelectric points.
Biological samples, such...
6.6K
Intrinsically Disordered Proteins02:18

Intrinsically Disordered Proteins

18.6K
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...
18.6K
SDS-PAGE01:27

SDS-PAGE

29.9K
Gel electrophoresis is a method that separates biological macromolecules like nucleic acids or proteins by forcing them to pass through a gel matrix under an electric field.
A variation of gel electrophoresis, termed  polyacrylamide gel electrophoresis (PAGE), is commonly used for separating proteins according to their molecular size by passing them through a polyacrylamide gel. Because of the varying charges associated with amino acid side chains, PAGE can be used to separate intact...
29.9K
What are Proteins?01:28

What are Proteins?

17.8K
Proteins are polymers of amino acids linked together by peptide bonds. Proteins and polypeptides are interchangeably used to refer to long chains of amino acids. However, polypeptides have a molecular weight of fewer than 10,000 daltons, while proteins have greater molecular weight.  Polypeptides with less than 20 amino acids are called oligopeptides or simply peptides. Interactions among the constituent amino acid side chains of proteins help them fold into a stable 3-dimensional...
17.8K
Overview of Protein Sorting and Transport01:45

Overview of Protein Sorting and Transport

16.6K
Eukaryotic cells have different membrane-bound organelles with distinct protein requirements. The process by which proteins are targeted to a specific organelle is called protein sorting.
Protein sorting can be of two types: signal-based sorting and vesicle-based trafficking. In signal-based sorting, specific amino acid sequences called sorting signals target proteins to the proper location inside the cell either via gated transport or by protein translocation.  In gated transport, folded...
16.6K
Phosphoinositides and PIPs01:42

Phosphoinositides and PIPs

8.9K
Phosphoinositides are a group of phospholipids containing a glycerol backbone with two fatty acid chains and a phosphate attached to a myoinositol sugar ring. The inositol head group extends into the cytoplasm, where it is modified by adding phosphate groups to form phosphatidylinositol phosphates or PIPs.
Different phosphoinositides are synthesized and recruited on the cytosolic face of the plasma membrane. The localization of specific phosphoinositides concentrated in separate membrane...
8.9K

You might also read

Related Articles

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

Sort by
Same author

Functional Roles of Src Kinase Activity in Oocyte Maturation and Artificial Egg Activation in <i>Xenopus laevis</i>.

Cells·2026
Same author

Compost fermented with thermophilic Bacillaceae reduces heat stress-induced mortality in laying hens through gut microbial modulation.

Animal microbiome·2026
Same author

The <i>Xenopus</i> Oocyte System: Molecular Dynamics of Maturation, Fertilization, and Post-Ovulatory Fate.

Biomolecules·2026
Same author

Maternal administration of octanoate, a medium-chain fatty acid, improves feed efficiency of Japanese black calves through influencing gut bacteriome structure.

Scientific reports·2025
Same author

Egg Overactivation-An Overlooked Phenomenon of Gamete Physiology.

International journal of molecular sciences·2025
Same author

Causal estimation of the relationship between reproductive performance and the fecal bacteriome in cattle.

Animal microbiome·2025

Related Experiment Video

Updated: Oct 9, 2025

Highly Sensitive and Quantitative Detection of Proteins and Their Isoforms by Capillary Isoelectric Focusing Method
07:58

Highly Sensitive and Quantitative Detection of Proteins and Their Isoforms by Capillary Isoelectric Focusing Method

Published on: September 19, 2018

6.8K

Protein pI and Intracellular Localization.

Alexander A Tokmakov1, Atsushi Kurotani2, Ken-Ichi Sato3

  • 1Department of Genetic Engineering, Faculty of Biology-Oriented Science and Technology, Kindai University, Wakayama, Japan.

Frontiers in Molecular Biosciences
|December 16, 2021
PubMed
Summary

Protein isoelectric point (pI) computational analysis reveals multimodal distributions across species proteomes. This multimodality is linked to subcellular localization, offering insights into protein function and cellular organization.

Keywords:
local environmentmultimodalityprotein pIproteome-wide analysissubcellular localization

More Related Videos

Separation of Bioactive Small Molecules, Peptides from Natural Sources and Proteins from Microbes by Preparative Isoelectric Focusing IEF Method
09:57

Separation of Bioactive Small Molecules, Peptides from Natural Sources and Proteins from Microbes by Preparative Isoelectric Focusing IEF Method

Published on: June 14, 2020

9.6K
Consensus Brain-derived Protein, Extraction Protocol for the Study of Human and Murine Brain Proteome Using Both 2D-DIGE and Mini 2DE Immunoblotting
10:51

Consensus Brain-derived Protein, Extraction Protocol for the Study of Human and Murine Brain Proteome Using Both 2D-DIGE and Mini 2DE Immunoblotting

Published on: April 10, 2014

16.3K

Related Experiment Videos

Last Updated: Oct 9, 2025

Highly Sensitive and Quantitative Detection of Proteins and Their Isoforms by Capillary Isoelectric Focusing Method
07:58

Highly Sensitive and Quantitative Detection of Proteins and Their Isoforms by Capillary Isoelectric Focusing Method

Published on: September 19, 2018

6.8K
Separation of Bioactive Small Molecules, Peptides from Natural Sources and Proteins from Microbes by Preparative Isoelectric Focusing IEF Method
09:57

Separation of Bioactive Small Molecules, Peptides from Natural Sources and Proteins from Microbes by Preparative Isoelectric Focusing IEF Method

Published on: June 14, 2020

9.6K
Consensus Brain-derived Protein, Extraction Protocol for the Study of Human and Murine Brain Proteome Using Both 2D-DIGE and Mini 2DE Immunoblotting
10:51

Consensus Brain-derived Protein, Extraction Protocol for the Study of Human and Murine Brain Proteome Using Both 2D-DIGE and Mini 2DE Immunoblotting

Published on: April 10, 2014

16.3K

Area of Science:

  • Bioinformatics
  • Proteomics
  • Computational Biology

Background:

  • The protein isoelectric point (pI) is a fundamental property calculable from amino acid sequences.
  • Computational pI predictions show good agreement with experimental data.
  • Whole-genome data enables large-scale proteome-wide pI distribution analyses.

Purpose of the Study:

  • To overview the multimodality of proteome-wide protein isoelectric point (pI) distributions across diverse organisms.
  • To investigate the relationship between protein pI and subcellular localization.
  • To discuss factors influencing intracellular localization-specific pI profiles.

Main Methods:

  • Computational analysis of amino acid sequences to determine protein isoelectric points (pI).
  • Comparative analysis of proteome-wide pI distributions from whole-genome sequences.
  • Statistical examination of pI distributions in relation to subcellular localization data.

Main Results:

  • Whole-proteome distributions of protein pI values exhibit multimodality in various species.
  • Subcellular localization-specific pI distributions contribute to the observed overall multimodality.
  • Distinct pI profiles are associated with different intracellular compartments.

Conclusions:

  • The multimodality of proteome-wide pI distributions is a conserved feature across species.
  • Subcellular localization is a key determinant of local pI profiles within the cell.
  • Understanding these relationships provides insights into protein function and cellular compartmentalization.