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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.
Conservative Site-specific Recombination and Phase Variation02:53

Conservative Site-specific Recombination and Phase Variation

Because the DNA segments are cut and reorganized in a direction-specific manner, site-specific recombination has emerged as an efficient genetic engineering technique. Flippase and Cyclization recombinases or Flp and Cre, respectively, are two members of the tyrosine recombinase family derived from bacteriophages, that are used to mediate site-specific DNA insertions, deletions, and targeted expression of proteins in mammalian cell lines.
The recognition sites for Cre recombinase called LoxP...
Ligand Binding and Linkage00:49

Ligand Binding and Linkage

Allosteric proteins have more than one ligand binding site; the binding of a ligand to any of these sites influences the binding of ligands to the other sites. When a protein is allosteric, its binding sites are called coupled or linked.  In the case of enzymes, the site that binds to the substrate is known as the active site and the other site is known as the regulatory site. When a ligand binds to the regulatory site, this leads to conformational changes in the protein that can influence the...
Transfer RNA Synthesis02:36

Transfer RNA Synthesis

One of the unique features of tRNA is the presence of modified bases. In some tRNAs, modified bases account for nearly 20% of the total bases in the molecule. Altogether, these unusual bases protect the tRNA from enzymatic degradation by RNases.
Each of these chemical modifications is carried by a specific enzyme, post-transcription. All of these enzymes have unique base and site-specificity. Methylation, the most common chemical modification, is carried by at least nine different enzymes, with...
Translational Regulation01:29

Translational Regulation

Translational regulation in prokaryotes ensures efficient protein synthesis by controlling ribosome access to mRNA. This regulation is mediated by secondary RNA structures, including translational riboswitches, RNA thermometers, and small RNAs (sRNAs), which respond to intracellular and environmental signals to modulate gene expression.Translational RiboswitchesRiboswitches in the leader region of mRNAs can regulate translation by altering the accessibility of the Shine-Dalgarno (SD) sequence,...
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 20, 2026

Simultaneous Affinity Enrichment of Two Post-Translational Modifications for Quantification and Site Localization
12:11

Simultaneous Affinity Enrichment of Two Post-Translational Modifications for Quantification and Site Localization

Published on: February 27, 2020

The rational parameterization theorem for multisite post-translational modification systems.

Matthew Thomson1, Jeremy Gunawardena

  • 1Biophysics Program, Harvard University, Cambridge, MA 02138, USA.

Journal of Theoretical Biology
|September 22, 2009
PubMed
Summary
This summary is machine-generated.

Studying protein post-translational modifications is complex due to numerous forms. This research simplifies analysis by using algebraic geometry to predict modification states from enzyme concentrations, enabling systems biology insights.

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Synthesizing Amino Acids Modified with Reactive Carbonyls in Silico to Assess Structural Effects Using Molecular Dynamics Simulations
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A Fast and Quantitative Method for Post-translational Modification and Variant Enabled Mapping of Peptides to Genomes
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A Fast and Quantitative Method for Post-translational Modification and Variant Enabled Mapping of Peptides to Genomes

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Related Experiment Videos

Last Updated: Jun 20, 2026

Simultaneous Affinity Enrichment of Two Post-Translational Modifications for Quantification and Site Localization
12:11

Simultaneous Affinity Enrichment of Two Post-Translational Modifications for Quantification and Site Localization

Published on: February 27, 2020

Synthesizing Amino Acids Modified with Reactive Carbonyls in Silico to Assess Structural Effects Using Molecular Dynamics Simulations
05:57

Synthesizing Amino Acids Modified with Reactive Carbonyls in Silico to Assess Structural Effects Using Molecular Dynamics Simulations

Published on: April 26, 2024

A Fast and Quantitative Method for Post-translational Modification and Variant Enabled Mapping of Peptides to Genomes
09:10

A Fast and Quantitative Method for Post-translational Modification and Variant Enabled Mapping of Peptides to Genomes

Published on: May 22, 2018

Area of Science:

  • Biochemistry and Systems Biology
  • Computational Biology
  • Chemical Kinetics

Background:

  • Post-translational modifications (PTMs) are crucial for cellular regulation.
  • Studying PTMs is challenging due to the exponential increase in substrate modification forms (modforms) with more sites.
  • Previous studies often used simplified models for biochemical networks.

Purpose of the Study:

  • To develop a generalized mathematical framework for analyzing biochemical networks of protein post-translational modifications.
  • To reduce the computational complexity of simulating PTM networks.
  • To enable new biological predictions and advance systems biology of PTMs.

Main Methods:

  • Modeling biochemical networks under mass-action kinetics with multiple substrates, modification types, and enzymes.
  • Utilizing general enzymatic mechanisms for forward and reverse reactions.
  • Applying algebraic geometry to parameterize steady-state modform concentrations using free enzyme concentrations and rate constants.

Main Results:

  • Steady-state modform concentrations form an algebraic variety.
  • This variety can be parameterized by rational functions of free enzyme concentrations.
  • Steady states can be calculated by solving L algebraic equations, a significant reduction from simulating differential equations.

Conclusions:

  • The developed parameterization dramatically reduces computational complexity, enabling analysis of previously intractable PTM networks.
  • This approach provides a foundation for systems biology of PTMs.
  • The study reveals deeper connections between biochemical networks and algebraic geometry.