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Related Concept Videos

Solution Composition During Acid/Base Titrations01:17

Solution Composition During Acid/Base Titrations

The titration of a weak acid with a strong base results in the formation of water and the conjugate base of the acid. For instance, titrating acetic acid with sodium hydroxide leads to the formation of water and sodium acetate. A solution of acetic acid and sodium acetate constitutes a buffer whose relative concentration at different stages of the titration is indicated by the α values, which represent percentages of the weak acid and its conjugate base.
The α0 and α1 values represent the...

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Quantification of Site-specific Protein Lysine Acetylation and Succinylation Stoichiometry Using Data-independent Acquisition Mass Spectrometry
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Quantitative analysis of S-acylation.

Carla Busquets Hernández1, Alexandra Tsiotsia1, Gemma Triola1

  • 1Institute for Advanced Chemistry of Catalonia (IQAC-CSIC), Barcelona, Spain.

Methods in Enzymology
|March 27, 2026
PubMed
Summary

S-acylation, a vital protein modification, involves attaching fatty acids to cysteine residues. This study introduces a new method to identify and quantify diverse fatty acids in S-acylated proteins, advancing our understanding of this crucial cellular process.

Keywords:
Fatty acidsHeterogeneousHydroxylaminePalmitoylationProtein lipidationS-acylation

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Background:

  • S-acylation is a reversible protein post-translational modification involving the attachment of fatty acids to cysteine residues.
  • This modification influences protein properties like membrane binding, localization, and interactions, impacting key cellular processes.
  • Dysfunctional S-acylation is linked to diseases such as cancer and neurodegeneration, highlighting its therapeutic potential.

Purpose of the Study:

  • To address the challenge of studying the heterogeneous lipid composition of S-acylated proteins.
  • To develop and report a method for identifying and quantifying diverse fatty acids attached to S-acylated proteins.

Main Methods:

  • The study reports a novel protocol for the identification and quantification of fatty acids in S-acylated proteins.
  • This method aims to overcome limitations in systematically studying heterogeneous lipid compositions.

Main Results:

  • The developed method enables the identification and quantification of various fatty acids involved in S-acylation.
  • This advances the systematic study of lipid diversity in S-acylated proteins.

Conclusions:

  • The new method facilitates a deeper understanding of S-acylation's role in regulating protein function.
  • This research opens avenues for exploring the therapeutic potential of targeting S-acylation pathways.