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Related Concept Videos

Mass Spectrometry: Complex Analysis01:21

Mass Spectrometry: Complex Analysis

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Mass spectrometry is an important technique for the identification of pure compounds. However, it has some limitations for the analysis of complex mixtures, often due to excessive fragmentation making the spectrum too complicated to decipher. Mass spectrometry can be combined with suitable separation methods in sequence, forming hyphenated methods, which are useful in the analysis of complex mixtures.
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Tandem mass spectrometry, also known as MS/MS or MS2, is an analytical technique that employs two mass analyzers. Essentially it is a series of mass spectrometers that helps isolate a particular biomolecule and then helps study its chemical properties.
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Inductively coupled plasma–mass spectrometry (ICP–MS) is a highly selective and sensitive technique for accurate elemental analysis. Though the analysis of ICP–MS mass spectra is comparatively straightforward, it is affected by spectroscopic and non-spectroscopic interferences. Spectroscopic interferences arise when the plasma contains ionic species with an m/z value the same as the analyte ion. Spectroscopic interference can be categorized as isobaric, polyatomic ions, and...
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Protein Complex Assembly

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Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types.  Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
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In inductively coupled plasma–mass spectrometry (ICP–MS), an inductively coupled plasma (ICP) torch is used as an atomizer and ionizer. Solid samples are dissolved and volatilized before being introduced into the high-temperature argon plasma, while solution samples are nebulized and passed through the high-temperature argon plasma. Plasma dissociates the analytes and ionizes their component atoms to form a mixture of positive ions and molecular species. The positive ions are then...
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G-protein coupled receptors are ligand binding receptors that indirectly affect changes in the cell. The actual receptor is a single polypeptide that transverses the cell membrane seven times creating intracellular and extracellular loops. The extracellular loops create a ligand specific pocket which binds to neurotransmitters or hormones. The intracellular loops holds onto the G-protein.
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Related Experiment Video

Updated: Feb 12, 2026

Identification of Inositol Phosphate or Phosphoinositide Interacting Proteins by Affinity Chromatography Coupled to Western Blot or Mass Spectrometry
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Identification of Signaling Protein Complexes by Parallel Affinity Precipitation Coupled with Mass Spectrometry.

Heng Lu1, Qishan Lin2, Jihe Zhao1

  • 1Burnett School of Biomedical Science, College of Medicine, University of Central Florida, Orlando, FL, USA.

Cell Communication Insights
|May 20, 2014
PubMed
Summary

We developed a new parallel affinity precipitation method for studying protein-protein interactions. This quick, economical, and specific assay overcomes limitations of previous techniques for analyzing cellular communication.

Keywords:
Myc tagco-immunoprecipitation (co-IP)hemagglutinin tagmass spectrometryparallel affinity precipitation (PAP)protein–protein interactiontandem affinity purification (TAP)

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Identification of Protein Complexes in Escherichia coli using Sequential Peptide Affinity Purification in Combination with Tandem Mass Spectrometry
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Area of Science:

  • Cellular biology
  • Molecular biology
  • Biochemistry

Background:

  • Protein-protein interactions are crucial for cellular signaling pathways.
  • Understanding these interactions provides insights into cell communication.
  • Existing methods like tandem affinity purification have limitations.

Purpose of the Study:

  • To develop a simplified, efficient, and specific assay for identifying protein-protein interactions.
  • To overcome the drawbacks of tandem affinity purification (TAP) procedures.

Main Methods:

  • A novel parallel affinity precipitation protocol was designed.
  • This method aims to avoid issues associated with epitope tags and large cell culture requirements.

Main Results:

  • The developed assay is quick, economical, and specific.
  • It offers an alternative to the time-consuming and potentially disruptive tandem affinity purification.

Conclusions:

  • The parallel affinity precipitation protocol is a valuable tool for studying protein complexes.
  • This method facilitates the identification of signaling protein complexes involved in cell communication.