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Related Concept Videos

Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein.
Protein Modifications in the RER01:26

Protein Modifications in the RER

Modification of secretory and transmembrane proteins entering the rough ER begins in the ER lumen. These modifications aid in protein folding and stabilize the acquired tertiary structure. Protein modifications in the rough ER co-occur at different stages of protein folding.
Broadly, these modifications can be categorized into four main categories — glycosylation, formation of disulfide bonds, assembly of protein subunits, and specific proteolytic cleavages like removal of signal sequences.
Regulated Protein Degradation02:58

Regulated Protein Degradation

It is vital to regulate the activity of enzymatic as well as non-enzymatic proteins inside the cell. This can be achieved either through creating a balance between their rate of synthesis and degradation or regulating the intrinsic activity of the protein. Both these regulation mechanisms play an essential role in the normal functioning of cells.
Protein degradation plays two important roles in the cells. It helps to protect cells from misfolded or damaged proteins before they lead to a...
Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...
Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...
Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...

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Related Experiment Video

Updated: Jun 23, 2026

In Vitro Analysis of E3 Ubiquitin Ligase Function
06:06

In Vitro Analysis of E3 Ubiquitin Ligase Function

Published on: May 14, 2021

Conformational transition associated with E1-E2 interaction in small ubiquitin-like modifications.

Jianghai Wang1, Brian Lee, Sheng Cai

  • 1Division of Immunology, Beckman Research Institute of the City of Hope, Duarte, California 91010, USA.

The Journal of Biological Chemistry
|May 16, 2009
PubMed
Summary

Small ubiquitin-like modifier E1 enzyme

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In Vitro Ubiquitination and Deubiquitination Assays of Nucleosomal Histones
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In Vitro Ubiquitination and Deubiquitination Assays of Nucleosomal Histones

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Detection of Protein Ubiquitination
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Detection of Protein Ubiquitination

Published on: August 19, 2009

Related Experiment Videos

Last Updated: Jun 23, 2026

In Vitro Analysis of E3 Ubiquitin Ligase Function
06:06

In Vitro Analysis of E3 Ubiquitin Ligase Function

Published on: May 14, 2021

In Vitro Ubiquitination and Deubiquitination Assays of Nucleosomal Histones
11:36

In Vitro Ubiquitination and Deubiquitination Assays of Nucleosomal Histones

Published on: July 25, 2019

Detection of Protein Ubiquitination
09:00

Detection of Protein Ubiquitination

Published on: August 19, 2009

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Structural Biology

Background:

  • Ubiquitin-like modifications are crucial for cellular functions.
  • Enzyme-substrate recognition, specifically E1-E2 interaction, is vital for these modifications.

Purpose of the Study:

  • To investigate the conformational dynamics of the E1 activating enzyme's E2-binding surface.
  • To elucidate the mechanism of E2 enzyme recognition by the E1 enzyme.

Main Methods:

  • Utilized biophysical techniques to study protein conformational states.
  • Employed mutagenesis to assess the functional impact of altered conformational dynamics.

Main Results:

  • Identified an E2-binding surface on E1 with significant ordered and disordered populations.
  • Observed a transition from a disordered to an ordered state upon E2 binding, facilitating molecular recognition.
  • Demonstrated that mutations disrupting this equilibrium lead to loss of function.

Conclusions:

  • Conformational flexibility and folding-upon-binding are critical for E1-E2 molecular recognition.
  • The dynamic nature of the E1 binding site resolves the Levinthal Paradox in protein folding.
  • This study underscores the importance of protein dynamics in biological processes.