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Related Concept Videos

Protein Kinases and Phosphatases02:54

Protein Kinases and Phosphatases

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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...
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[3,3] Sigmatropic Rearrangement of 1,5-Dienes: Cope Rearrangement01:21

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The Cope rearrangement is classified as a [3,3] sigmatropic shift in 1,5-dienes, leading to a more stable, isomeric 1,5-diene. The reaction involves a concerted movement of six electrons, four from two π bonds and two from a σ bond, via an energetically favorable chair-like transition state.
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Throughout its ~4.5 billion year history, the Earth has experienced periods of warming and cooling. However, the current drastic increase in global temperatures is well outside of the Earth’s cyclic norms, and evidence for human-caused global climate change is compelling. Paleoclimatology, the study of ancient climate conditions, provides ample evidence for human-caused global climate change by comparing recent conditions with those in the past.
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Compounds bearing two hydroxyl groups are known as diols. When the hydroxyl groups are located on adjacent carbon atoms, the diols are called vicinal diols or glycols. Under acidic conditions, vicinal diols undergo a specific reaction called pinacol rearrangement.
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Related Experiment Video

Updated: Jan 21, 2026

Quantification of Bacterial Histidine Kinase Autophosphorylation Using a Nitrocellulose Binding Assay
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Autophosphorylation activates c-Src kinase through global structural rearrangements.

Edgar E Boczek1, Qi Luo2, Marco Dehling3

  • 1Center for Integrated Protein Science, Department Chemie, Technische Universität München, 85748 Garching, Germany; Max Planck Institute of Molecular Cell Biology and Genetics, 01307 Dresden, Germany.

The Journal of Biological Chemistry
|July 24, 2019
PubMed
Summary

Autophosphorylation of c-Src kinase stabilizes the ATP binding site, increasing enzymatic activity. This process involves domain rearrangements and increased kinase domain rigidity for signal transduction.

Keywords:
ATPSrcactivationbiophysicsconformational changeenzyme mechanismhydrogen/deuterium exchangemolecular dynamicsoncogenephosphorylationprotein kinase

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Molecular Biology

Background:

  • c-Src is a key kinase in signal transduction, regulated by phosphorylation.
  • Autophosphorylation is crucial for c-Src activation, but its structural effects are unclear.

Purpose of the Study:

  • To elucidate the structural changes in c-Src during nucleotide binding and Tyr416 autophosphorylation.
  • To understand the molecular mechanisms of c-Src kinase activation.

Main Methods:

  • Biochemical experiments
  • Hydrogen/deuterium exchange mass spectrometry (HDX-MS)
  • Atomistic molecular dynamics simulations

Main Results:

  • Autophosphorylation causes large domain rearrangements and displacement of regulatory domains.
  • The kinase domain becomes more rigid, stabilizing the ATP binding site.
  • Enzymatic activity of c-Src increases four-fold upon autophosphorylation.

Conclusions:

  • A molecular framework for c-Src kinase regulation via autophosphorylation is provided.
  • Findings offer insights into general kinase activation mechanisms.