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Related Concept Videos

Protein Complex Assembly02:41

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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A sizable fraction of proteins destined for ER are first synthesized in the cell cytosol and then transported across the ER membrane–a process called post-translational translocation. Similar to cotranslationally translocated proteins, these proteins also use the Sec translocon complex to enter the ER lumen.
Targeting proteins to the ER
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Heterotrimeric G proteins are guanine nucleotide-binding proteins. As the name suggests, heterotrimeric G proteins are composed of three subunits: alpha, beta, and gamma. They remain GDP-bound or GTP-bound inside the cells and switch between inactive/active states. The Gα subunit possesses the nucleotide-binding pocket that binds guanine nucleotides and switches between GDP or GTP-bound states. In contrast, the Gꞵ and Gγ subunits are always bound together with high...
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The translocon complex situated on the ER membrane is the main gateway for the protein secretory pathway. It facilitates the transport of nascent peptides into the ER lumen and their insertion into the ER membrane.
Sec61 protein conducting channel
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Nuclear Protein Sorting01:34

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Nuclear protein sorting is the selective trafficking of histones, polymerases, gene regulatory proteins into the nucleus and exporting RNAs and ribosomes to the cytosol. It is a tightly controlled process that regulates gene expression within a cell.
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Directing Proteins to the Rough Endoplasmic Reticulum

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The organelle-specific signaling sequences direct proteins synthesized in the cytosol to their final destination like ER, mitochondria, peroxisomes, etc. Some of the proteins directed to ER are then trafficked via vesicles to other organelles within the cell or the extracellular environment through the Golgi complex. For example, the rough ER synthesizes soluble proteins for transportation to the lysosomes or secretion out of the cell. It can also synthesize transmembrane proteins that can...
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Related Experiment Video

Updated: Nov 29, 2025

Analyzing Protein Architectures and Protein-Ligand Complexes by Integrative Structural Mass Spectrometry
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Analyzing Protein Architectures and Protein-Ligand Complexes by Integrative Structural Mass Spectrometry

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Releasing Nonperipheral Subunits from Protein Complexes in the Gas Phase.

Guanbo Wang1, Lingxiao Chaihu1,2, Meng Tian3

  • 1School of Chemistry and Materials Science, Nanjing Normal University, 210023 Nanjing, China.

Analytical Chemistry
|November 19, 2020
PubMed
Summary
This summary is machine-generated.

Native mass spectrometry and tandem mass spectrometry reveal how nonperipheral subunits are released from protein complexes. This provides new insights into protein complex stoichiometry and topology.

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Analyzing Dynamic Protein Complexes Assembled On and Released From Biolayer Interferometry Biosensor Using Mass Spectrometry and Electron Microscopy
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Area of Science:

  • Biochemistry
  • Structural Biology
  • Analytical Chemistry

Background:

  • Protein quaternary structure is crucial for function.
  • Native mass spectrometry preserves protein complexes in the gas phase.
  • Tandem mass spectrometry (CID) analyzes subunit release for structural information.

Purpose of the Study:

  • To investigate dissociation pathways of nonperipheral subunits in hetero-complexes using CID.
  • To explore how releasing nonperipheral subunits provides unique structural data.

Main Methods:

  • Native mass spectrometry to maintain complex integrity.
  • Tandem mass spectrometry with collision-induced dissociation (CID) at high energies.
  • Analysis of dissociation pathways for various protein assemblies.

Main Results:

  • Demonstrated preferential release of peripheral subunits during CID.
  • Identified pathways for nonperipheral subunit release, including sequential dissociation and direct ejection.
  • Showed nonperipheral subunits can be released from charge-reduced or elongated complexes.

Conclusions:

  • Controlled CID can release nonperipheral subunits, offering unique structural insights.
  • Understanding these dissociation pathways enhances knowledge of protein complex stoichiometry and topology.