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Related Concept Videos

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...
Allosteric Proteins-ATCase01:19

Allosteric Proteins-ATCase

Binding sites linkages can regulate a protein's function.  For example, enzyme activity is often regulated through a feedback mechanism where the end product of the biochemical process serves as an inhibitor.
Aspartate transcarbamoylase (ATCase) is a cytosolic enzyme that catalyzes the condensation of L-aspartate and carbamoyl phosphate to  N-carbamoyl-L-aspartate. This reaction is the first step in pyrimidine biosynthesis. UTP and CTP, the end products of the pyrimidine synthesis pathway,...
Phosphorylation01:02

Phosphorylation

The addition or removal of phosphate groups from proteins is the most common chemical modification that regulates cellular processes. These modifications can affect the structure, activity, stability, and localization of proteins within cells as well as their interactions with other proteins.
During phosphorylation, protein kinases transfer the terminal phosphate group of ATP to specific amino acid side chains of substrate proteins. Serine, threonine, and tyrosine are the most commonly...
Phosphorylation01:02

Phosphorylation

The addition or removal of phosphate groups from proteins is the most common chemical modification that regulates cellular processes. These modifications can affect the structure, activity, stability, and localization of proteins within cells as well as their interactions with other proteins.
During phosphorylation, protein kinases transfer the terminal phosphate group of ATP to specific amino acid side chains of substrate proteins. Serine, threonine, and tyrosine are the most commonly...

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Related Experiment Video

Updated: Jun 22, 2026

Oligopeptide Competition Assay for Phosphorylation Site Determination
09:16

Oligopeptide Competition Assay for Phosphorylation Site Determination

Published on: May 18, 2017

Unlimited multistability in multisite phosphorylation systems.

Matthew Thomson1, Jeremy Gunawardena

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

Nature
|June 19, 2009
PubMed
Summary
This summary is machine-generated.

Multisite protein phosphorylation, a key regulatory mechanism, can generate complex signaling networks. This study reveals that opposing enzymes create distinct, stable distributions of protein phospho-forms, enabling flexible cellular information processing.

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Last Updated: Jun 22, 2026

Oligopeptide Competition Assay for Phosphorylation Site Determination
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Published on: May 18, 2017

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A Mass Spectrometry-Based Approach to Identify Phosphoprotein Phosphatases and their Interactors

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Identification of Cyclin-dependent Kinase 1 Specific Phosphorylation Sites by an In Vitro Kinase Assay
12:26

Identification of Cyclin-dependent Kinase 1 Specific Phosphorylation Sites by an In Vitro Kinase Assay

Published on: May 3, 2018

Area of Science:

  • Biochemistry and Molecular Biology
  • Systems Biology
  • Posttranslational Modifications

Background:

  • Reversible protein phosphorylation is a crucial posttranslational modification, with eukaryotes exhibiting significantly more phosphorylation sites per protein than prokaryotes.
  • Multisite phosphorylation generates an exponential number of protein phospho-forms, each potentially having distinct biological roles.
  • The regulation and distribution of these diverse phospho-forms within a cell have remained largely unknown.

Purpose of the Study:

  • To investigate the steady-state distributions of phospho-forms for multisite substrates under opposing kinase and phosphatase activity.
  • To explore the regulatory potential and information processing capabilities of complex phospho-proteomes.
  • To develop a simplified mathematical framework for analyzing multisite phosphorylation dynamics.

Main Methods:

  • Mathematical modeling of opposing kinase and phosphatase activities on multisite substrates.
  • Analysis of the geometric properties of steady-state phospho-form concentrations.
  • Derivation of algebraic equations to replace complex differential equation simulations.

Main Results:

  • Opposing enzyme action on multisite substrates can lead to distinct stable phospho-form distributions at steady state.
  • The number of stable distributions increases with the number of phosphorylation sites (n).
  • Phospho-form distributions can be focused or diffuse, suggesting a fluid regulatory network capable of encoding information.

Conclusions:

  • The plasticity of phospho-form distributions provides a mechanism for complex information processing in eukaryotic cells.
  • A large number of phosphorylation sites may confer a functional advantage by increasing regulatory potential.
  • A novel mathematical approach simplifies the analysis of multisite phosphorylation, applicable to complex posttranslational modification networks.