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

Two-dimensional Gel Electrophoresis

Two-dimensional Gel Electrophoresis

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...

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...

SDS-PAGE

SDS-PAGE

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...

Protein Folding

Protein Folding

Proteins are chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation, critical to its biological function. Interactions between its constituent amino acids guide protein folding, and hence the protein structure is primarily dependent on its amino acid sequence.
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...

Protein Folding

Protein Folding

You might also read

Related Articles

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

Sort by

Same author

Hydrogels with programmed spatiotemporal mechanical cues for stem cell-assisted bone regeneration.

Nature communications·2025

Same author

Hydrogels with prestressed tensegrity structures.

Nature communications·2025

Same author

[Cadmium Content Characteristics, Health Risk Assessment, and Soil Environmental Benchmarks in Farmland Soil and Agricultural Products in Ningxia].

Huan jing ke xue= Huanjing kexue·2025

Same author

Ecological evolution in a semi-arid lake: insights from subfossil diatoms and geochemical indicators in Hulun Lake.

Frontiers in microbiology·2025

Same author

Study on the Effects of Vibration Force Field on the Mixing and Structural Properties of PLA/PBS/EGMA Blends.

Polymers·2025

Same author

Zirconium metal-organic cages for iodine adsorption: Effect of substituted groups and pore structures.

Journal of colloid and interface science·2025

Same journal

OpenIMC: an open-source platform for analyzing single-cell and spatial proteomics by imaging mass cytometry.

BMC bioinformatics·2026

Same journal

NAP: an open source pipeline for cross-domain microbiome profiling using Nanopore sequencing-derived amplicon data.

BMC bioinformatics·2026

Same journal

SurvGME: an R package for survival analysis with graphical and measurement error models.

BMC bioinformatics·2026

Same journal

SimMapNet: a Bayesian framework for gene regulatory network inference using gene ontology similarities as external hint.

BMC bioinformatics·2026

Same journal

Dual channel drug-drug interactions extraction based on cross attention.

BMC bioinformatics·2026

Same journal

FeSseqdb: a curated sequence-level database and interpretable machine learning framework for identifying iron-sulfur proteins.

BMC bioinformatics·2026

See all related articles

Search research articles

Related Experiment Video

Updated: Apr 19, 2026

Analysis of AtHIRD11 Intrinsic Disorder and Binding Towards Metal Ions by Capillary Gel Electrophoresis and Affinity Capillary Electrophoresis

Analysis of AtHIRD11 Intrinsic Disorder and Binding Towards Metal Ions by Capillary Gel Electrophoresis and Affinity Capillary Electrophoresis

Published on: August 22, 2018

Improving protein order-disorder classification using charge-hydropathy plots.

Fei Huang, Christopher J Oldfield, Bin Xue

BMC Bioinformatics

|January 7, 2015

Summary

This summary is machine-generated.

The charge-hydropathy plot

More Related Videos

Capillary Electrophoresis-based Hydrogen/Deuterium Exchange for Conformational Characterization of Proteins with Top-down Mass Spectrometry

Capillary Electrophoresis-based Hydrogen/Deuterium Exchange for Conformational Characterization of Proteins with Top-down Mass Spectrometry

Published on: June 8, 2021

Investigating Protein Sequence-structure-dynamics Relationships with Bio3D-web

Investigating Protein Sequence-structure-dynamics Relationships with Bio3D-web

Published on: July 16, 2017

Related Experiment Videos

Last Updated: Apr 19, 2026

Analysis of AtHIRD11 Intrinsic Disorder and Binding Towards Metal Ions by Capillary Gel Electrophoresis and Affinity Capillary Electrophoresis

Analysis of AtHIRD11 Intrinsic Disorder and Binding Towards Metal Ions by Capillary Gel Electrophoresis and Affinity Capillary Electrophoresis

Published on: August 22, 2018

Capillary Electrophoresis-based Hydrogen/Deuterium Exchange for Conformational Characterization of Proteins with Top-down Mass Spectrometry

Capillary Electrophoresis-based Hydrogen/Deuterium Exchange for Conformational Characterization of Proteins with Top-down Mass Spectrometry

Published on: June 8, 2021

Investigating Protein Sequence-structure-dynamics Relationships with Bio3D-web

Investigating Protein Sequence-structure-dynamics Relationships with Bio3D-web

Published on: July 16, 2017

Area of Science:

Protein bioinformatics
Computational biology
Biophysics

Background:

The earliest protein disorder predictor, the charge-hydropathy (C-H) plot, used the Kyte-Doolittle hydropathy scale.
The performance of the C-H plot in distinguishing structured from intrinsically disordered proteins (IDPs) may be improved by alternative scales.

Purpose of the Study:

To evaluate alternative hydropathy scales for improving the C-H plot's predictive performance.
To develop a novel hydropathy scale optimized for IDP prediction.

Main Methods:

Compared 19 hydropathy scales using the C-H plot's classification accuracy.
Developed and tested a new scale, IDP-Hydropathy, on a dataset of structured proteins and IDPs.

Main Results:

The Guy hydropathy scale improved C-H plot performance over the original Kyte-Doolittle scale.
The novel IDP-Hydropathy scale achieved 90% accuracy in classifying structured proteins and IDPs, surpassing existing scales.
IDP-Hydropathy showed strong correlation with other scales, indicating specificity to hydropathy.

Conclusions:

The IDP-Hydropathy scale offers superior performance for predicting protein disorder.
This new scale is recommended for algorithms aimed at disorder prediction.