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Related Concept Videos

Protein Complex Assembly02:41

Protein Complex Assembly

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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Related Experiment Video

Updated: May 24, 2026

Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy
14:55

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Published on: September 17, 2017

Determining the architectures of macromolecular assemblies.

Frank Alber1, Svetlana Dokudovskaya, Liesbeth M Veenhoff

  • 1Department of Bioengineering and Therapeutic Sciences, and California Institute for Quantitative Biosciences, Byers Hall, Suite 503B, 1700 4th Street, University of California at San Francisco, San Francisco, California 94158-2330, USA.

Nature
|November 30, 2007
PubMed
Summary

This study presents a new method using proteomic data to map the architecture of macromolecular assemblies, like the nuclear pore complex (NPC). This approach reveals detailed cellular structures and their principles.

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Area of Science:

  • Cellular Biology
  • Structural Biology
  • Biophysics

Background:

  • Understanding cellular machinery requires knowledge of macromolecular assembly structures.
  • The nuclear pore complex (NPC) is a large, complex assembly crucial for nuclear transport.

Purpose of the Study:

  • To develop and demonstrate a method for determining macromolecular assembly structures using proteomic data.
  • To map the architecture of the yeast nuclear pore complex (NPC).

Main Methods:

  • Collecting diverse, high-quality proteomic data.
  • Translating proteomic data into spatial restraints.
  • Using optimization algorithms to generate structural ensembles consistent with data.

Main Results:

  • A detailed architectural map of the yeast NPC was generated.
  • The structure revealed the configuration of NPC proteins.
  • Insights into NPC evolution and architectural principles were gained.

Conclusions:

  • Proteomic data can be effectively used to determine the architecture of complex macromolecular assemblies.
  • The developed approach provides a powerful tool for structural biology.
  • This method is broadly applicable to various macromolecular assemblies beyond the NPC.