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Related Concept Videos

Intrinsically Disordered Proteins02:18

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...
Protein-protein Interfaces02:04

Protein-protein Interfaces

Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a polypeptide...
Protein-Protein Interfaces02:04

Protein-Protein Interfaces

Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a polypeptide...
Fibrous Proteins00:55

Fibrous Proteins

Fibrous proteins are either long and narrow proteins or assemble to form long and thin structures. They contain repetitive units and usually consist of either alpha helices or beta sheets and, in rare cases, a mix of both. The amino acids in the primary structure often consist of repeating amino acid sequences. The role of fibrous proteins is primarily structural. Many are located in the extracellular matrix and are present in connective tissues to impart strength and joint mobility. They are...
Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
The...
Protein Folding01:22

Protein Folding

Overview

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Updated: Jun 23, 2026

Evaluation of Protein–Protein Interactions using an On-Membrane Digestion Technique
07:07

Evaluation of Protein–Protein Interactions using an On-Membrane Digestion Technique

Published on: July 19, 2019

Difficult proteins.

Ben Herbert1, Elizabeth Harry

  • 1Department of Medical and Molecular Biosciences, University of Technology, Sydney, 15 Broadway, Ultimo, Sydney, NSW 2007, Australia.

Methods in Molecular Biology (Clifton, N.J.)
|April 22, 2009
PubMed
Summary
This summary is machine-generated.

Proteomics analysis requires advanced techniques to capture diverse proteins. Combining multiple extraction, separation, and mass spectrometry methods improves the detection of low-abundance and challenging proteins.

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Mapping Dysfunctional Protein-Protein Interactions in Disease
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Mapping Dysfunctional Protein-Protein Interactions in Disease

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Multimer-PAGE: A Method for Capturing and Resolving Protein Complexes in Biological Samples
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Multimer-PAGE: A Method for Capturing and Resolving Protein Complexes in Biological Samples

Published on: May 5, 2017

Related Experiment Videos

Last Updated: Jun 23, 2026

Evaluation of Protein–Protein Interactions using an On-Membrane Digestion Technique
07:07

Evaluation of Protein–Protein Interactions using an On-Membrane Digestion Technique

Published on: July 19, 2019

Mapping Dysfunctional Protein-Protein Interactions in Disease
09:39

Mapping Dysfunctional Protein-Protein Interactions in Disease

Published on: October 24, 2025

Multimer-PAGE: A Method for Capturing and Resolving Protein Complexes in Biological Samples
07:40

Multimer-PAGE: A Method for Capturing and Resolving Protein Complexes in Biological Samples

Published on: May 5, 2017

Area of Science:

  • Proteomics
  • Biochemistry
  • Analytical Chemistry

Background:

  • Organismal proteomes exhibit vast protein diversity and dynamic range, making comprehensive analysis challenging with single methods.
  • Low-abundance, membrane, and alkaline proteins are often under-represented in standard proteome analyses.
  • Technological advancements in fractionation have focused on reducing sample complexity for improved protein detection.

Purpose of the Study:

  • To highlight the necessity of advanced techniques for comprehensive proteome analysis.
  • To discuss the role of fractionation in improving the detection of under-represented proteins.
  • To outline the components of a modern, effective proteomics platform.

Main Methods:

  • Utilizing multiple protein extraction strategies.
  • Employing various gel and chromatographic separation techniques.
  • Integrating diverse mass spectrometry (MS) analysis methods.

Main Results:

  • Fractionation reduces proteome complexity, enabling detailed study of sub-proteomes.
  • Improved detection of low-abundance and difficult-to-analyze proteins is achieved.
  • A multi-faceted approach is essential for comprehensive proteomic coverage.

Conclusions:

  • No single method can capture the entire proteome due to inherent biological complexity.
  • Modern proteomics relies on combining multiple extraction, separation, and analysis techniques.
  • Effective proteome analysis requires significant starting material and sophisticated methodologies.