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Related Concept Videos

Protein Kinases and Phosphatases02:54

Protein Kinases and Phosphatases

13.9K
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...
13.9K
Dynamic Equilibrium02:20

Dynamic Equilibrium

57.5K
A reversible chemical reaction represents a chemical process that proceeds in both forward (left to right) and reverse (right to left) directions. When the rates of the forward and reverse reactions are equal, the concentrations of the reactant and product species remain constant over time and the system is at equilibrium. A special double arrow is used to emphasize the reversible nature of the reaction. The relative concentrations of reactants and products in equilibrium systems vary greatly;...
57.5K
The Equilibrium Binding Constant and Binding Strength02:18

The Equilibrium Binding Constant and Binding Strength

14.3K
The equilibrium binding constant (Kb) quantifies the strength of a protein-ligand interaction. Kb can be calculated as follows when the reaction is at equilibrium:
14.3K
Amplifying Signals via Enzymatic Cascade01:22

Amplifying Signals via Enzymatic Cascade

14.2K
When a ligand binds to a cell-surface receptor, the receptor's intracellular domain changes shape, which may either activate its enzyme function or allow its binding to other molecules. The initial signal is amplified by most signal transduction pathways. This means that a single ligand molecule can activate multiple molecules of a downstream target. Proteins that relay a signal are most commonly phosphorylated at one or more sites, activating or inactivating the protein. Kinases catalyze...
14.2K
Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

8.3K
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...
8.3K
Phosphorylation01:02

Phosphorylation

52.5K
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...
52.5K

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Related Experiment Video

Updated: Oct 23, 2025

Assaying Protein Kinase Activity with Radiolabeled ATP
08:05

Assaying Protein Kinase Activity with Radiolabeled ATP

Published on: May 26, 2017

18.7K

Dynamic equilibria in protein kinases.

Laurel M Pegram1, Jake W Anderson1, Natalie G Ahn1

  • 1Department of Biochemistry, The University of Colorado at Boulder, USA.

Current Opinion in Structural Biology
|August 23, 2021
PubMed
Summary

Protein kinase activation and ligand binding involve structural changes. Recent solution studies reveal how these processes alter protein dynamics and allosteric signaling within kinases.

Area of Science:

  • Biochemistry
  • Structural Biology
  • Biophysics

Background:

  • X-ray crystallography has elucidated static structural changes in protein kinase activation and ligand binding.
  • Understanding the dynamic and energetic aspects of these processes remains a key challenge in kinase research.

Purpose of the Study:

  • To integrate structural data with solution studies to understand protein kinase dynamics.
  • To investigate how activation mechanisms and ligand binding influence kinase internal motions and allosteric regulation.

Main Methods:

  • Nuclear Magnetic Resonance (NMR) spectroscopy
  • Electron Paramagnetic Resonance (EPR) spectroscopy
  • Hydrogen-Deuterium Exchange Mass Spectrometry (HX-MS)
  • Fluorescence spectroscopy

More Related Videos

Characterization at the Molecular Level using Robust Biochemical Approaches of a New Kinase Protein
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Characterization at the Molecular Level using Robust Biochemical Approaches of a New Kinase Protein

Published on: June 30, 2019

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Identification of Kinase-substrate Pairs Using High Throughput Screening
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Identification of Kinase-substrate Pairs Using High Throughput Screening

Published on: August 29, 2015

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Related Experiment Videos

Last Updated: Oct 23, 2025

Assaying Protein Kinase Activity with Radiolabeled ATP
08:05

Assaying Protein Kinase Activity with Radiolabeled ATP

Published on: May 26, 2017

18.7K
Characterization at the Molecular Level using Robust Biochemical Approaches of a New Kinase Protein
11:23

Characterization at the Molecular Level using Robust Biochemical Approaches of a New Kinase Protein

Published on: June 30, 2019

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Identification of Kinase-substrate Pairs Using High Throughput Screening
11:13

Identification of Kinase-substrate Pairs Using High Throughput Screening

Published on: August 29, 2015

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Main Results:

  • Solution studies reveal the energetics and dynamics of multistate conformational ensembles in kinases.
  • Activation and ligand binding are shown to modulate internal protein motions.
  • Allosteric coupling between distant regulatory regions and the active site is facilitated by altered dynamics.

Conclusions:

  • Protein kinase function is critically dependent on dynamic conformational ensembles.
  • Ligand binding and activation trigger specific changes in protein dynamics, enabling allosteric communication.
  • Integrating structural and solution dynamics data provides a comprehensive view of kinase mechanisms.