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Related Concept Videos

Protein Folding01:22

Protein Folding

Overview
Protein Folding01:25

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 Folding01:22

Protein Folding

Overview
Proteomics01:33

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...
The Proteasome02:18

The Proteasome

Eukaryotic cells can degrade proteins through several pathways. One of the most important amongst these is the ubiquitin-proteasome pathway. It helps the cell eliminate the misfolded, damaged, or unwarranted cytoplasmic proteins in a highly specific manner.
In this pathway, the target proteins are first tagged with small proteins called ubiquitin. A series of enzymes carry out the ubiquitination of the target proteins - E1 (ubiquitin-activating enzyme), E2 (ubiquitin-conjugating enzyme), and E3...
The Proteasome01:13

The Proteasome

Eukaryotic cells can degrade proteins through several pathways. One of the most important among these is the ubiquitin-proteasome pathway. It helps the cell eliminate the misfolded, damaged, or unwarranted cytoplasmic proteins in a highly specific manner.
In this pathway, the target proteins are first tagged with small proteins called ubiquitin. This involves participation of a series of enzymes including— E1 (ubiquitin-activating enzyme), E2 (ubiquitin-conjugating enzyme), and E3 (ubiquitin...

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Related Experiment Video

Updated: May 10, 2026

Deep Proteome Profiling by Isobaric Labeling, Extensive Liquid Chromatography, Mass Spectrometry, and Software-assisted Quantification
10:37

Deep Proteome Profiling by Isobaric Labeling, Extensive Liquid Chromatography, Mass Spectrometry, and Software-assisted Quantification

Published on: November 15, 2017

Folding the proteome.

Esther Braselmann1, Julie L Chaney, Patricia L Clark

  • 1Department of Chemistry and Biochemistry, University of Notre Dame, Notre Dame, IN 46556 USA.

Trends in Biochemical Sciences
|June 15, 2013
PubMed
Summary
This summary is machine-generated.

Understanding protein folding is crucial for cell function, but current models are limited. New methods are needed to study diverse protein folding mechanisms in vivo, linking folding to disease and evolution.

Related Experiment Videos

Last Updated: May 10, 2026

Deep Proteome Profiling by Isobaric Labeling, Extensive Liquid Chromatography, Mass Spectrometry, and Software-assisted Quantification
10:37

Deep Proteome Profiling by Isobaric Labeling, Extensive Liquid Chromatography, Mass Spectrometry, and Software-assisted Quantification

Published on: November 15, 2017

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Structural Biology

Background:

  • Protein folding is fundamental to protein and cellular function.
  • Current understanding relies on studies of small, reversibly refolding proteins.
  • Limitations exist in predicting protein structures and mutation effects.

Purpose of the Study:

  • To highlight the need for new methods to study protein folding.
  • To emphasize the importance of investigating a broader range of proteins.
  • To connect protein folding mechanisms to disease and evolution.

Main Methods:

  • The abstract does not specify experimental or theoretical methods.
  • It calls for the development of novel quantitative approaches.
  • Focus is on studying protein folding under in vivo conditions.

Main Results:

  • Current model proteins do not represent the full complexity of proteomes.
  • Existing methods are insufficient for predicting structure and mutation impact.
  • A gap exists in understanding diverse in vivo folding mechanisms.

Conclusions:

  • New theoretical and experimental methods are urgently required.
  • Studying a broader set of proteins is essential for a comprehensive framework.
  • This research aims to link protein folding to disease, cell function, and evolution.