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Related Concept Videos

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...
Protein Kinases and Phosphatases02:54

Protein Kinases and Phosphatases

Proteins undergo chemical modifications that trigger changes in the charge, structure, and conformation of the proteins. Phosphorylation, acetylation, glycosylation, nitrosylation, ubiquitination, lipidation, methylation, and proteolysis are various protein modifications that regulate protein activity. Such modifications are usually enzyme-driven.
Protein kinases
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...
Protein Kinases and Phosphatases02:54

Protein Kinases and Phosphatases

Proteins undergo chemical modifications that trigger changes in the charge, structure, and conformation of the proteins. Phosphorylation, acetylation, glycosylation, nitrosylation, ubiquitination, lipidation, methylation, and proteolysis are various protein modifications that regulate protein activity. Such modifications are usually enzyme-driven.
Protein kinases
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...
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

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Visualizing the Conformational Dynamics of Membrane Receptors Using Single-Molecule FRET
10:59

Visualizing the Conformational Dynamics of Membrane Receptors Using Single-Molecule FRET

Published on: August 17, 2022

Conformational switching upon phosphorylation: a predictive framework based on energy landscape principles.

Joachim Lätzer1, Tongye Shen, Peter G Wolynes

  • 1Department of Chemistry & Biochemistry, University of California, San Diego, NSF Center for Theoretical Biological Physics, La Jolla, California 92093-0365, USA.

Biochemistry
|January 18, 2008
PubMed
Summary
This summary is machine-generated.

Post-translational phosphorylation alters protein structure by changing free energy landscapes. A new computational method predicts these conformational changes, improving our understanding of protein dynamics.

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Nuclear Magnetic Resonance Spectroscopy for the Identification of Multiple Phosphorylations of Intrinsically Disordered Proteins
12:47

Nuclear Magnetic Resonance Spectroscopy for the Identification of Multiple Phosphorylations of Intrinsically Disordered Proteins

Published on: December 27, 2016

Related Experiment Videos

Last Updated: Jul 8, 2026

Visualizing the Conformational Dynamics of Membrane Receptors Using Single-Molecule FRET
10:59

Visualizing the Conformational Dynamics of Membrane Receptors Using Single-Molecule FRET

Published on: August 17, 2022

Nuclear Magnetic Resonance Spectroscopy for the Identification of Multiple Phosphorylations of Intrinsically Disordered Proteins
12:47

Nuclear Magnetic Resonance Spectroscopy for the Identification of Multiple Phosphorylations of Intrinsically Disordered Proteins

Published on: December 27, 2016

Area of Science:

  • Protein dynamics
  • Computational biology
  • Biochemistry

Background:

  • Post-translational modifications, such as phosphorylation, are crucial for protein function.
  • Understanding how these modifications affect protein structure and dynamics is essential for deciphering biological processes.

Purpose of the Study:

  • To investigate the impact of phosphorylation on protein free energy landscapes and global conformation.
  • To develop and validate a computational method for predicting phosphorylated protein structures.

Main Methods:

  • Utilized a computational model incorporating free energy landscapes of phosphorylated and unphosphorylated states.
  • Applied principal component analysis and linear response theory to analyze conformational changes.
  • Developed a partially guided structure prediction Hamiltonian using transferable potentials.

Main Results:

  • Phosphorylation significantly alters free energy landscapes, with varying conformational transition barriers for different proteins (cystatin vs. NtrC).
  • NtrC likely undergoes partial unfolding for conformational transitions, while cystatin shows a larger energy cost.
  • The developed guided Hamiltonian accurately predicts global conformational changes induced by phosphorylation.

Conclusions:

  • Phosphorylation-induced conformational changes are governed by alterations in protein interaction potentials.
  • The novel computational approach enables accurate prediction of phosphorylated protein structures from unphosphorylated states (and vice versa).
  • This work provides a powerful tool for studying the structural consequences of post-translational modifications.