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Related Concept Videos

Protein Organization01:24

Protein Organization

Proteins are polymers of amino acid residues. They are versatile and responsible for different cellular functions, including DNA replication, molecular transport, catalysis, and structural support. Proteins have a hierarchical structure comprising at least three levels of organization: primary, secondary, and tertiary structure. Some large proteins have a quaternary structure where individual protein subunits are linked together.
The primary structure of a protein is its amino acid sequence.
Electron Microscope Tomography and Single-particle Reconstruction01:07

Electron Microscope Tomography and Single-particle Reconstruction

Transmission electron microscopy (TEM) can be used to determine the 3D structure of biological samples with the help of techniques such as electron microscope tomography and single-particle reconstruction. While single-particle reconstruction can examine macromolecules and macromolecular complexes in vitro conditions only, tomography permits the study of cell components or small cells in vivo.
Electron Tomography
Electron tomography can be performed either in TEM or STEM (scanning transmission...
Determination of Crystal Structures01:29

Determination of Crystal Structures

In the late 1800s, the revelation that light extended beyond visible wavelengths led to the discovery of X-rays by Wilhelm Roentgen. Recognized as high-energy electromagnetic radiation with short wavelengths, X-rays prompted exploration into their interaction with crystals. Max von Laue proposed in 1912 that the periodic arrangement of atoms, ions, or molecules in crystals would cause them to diffract X-rays, a hypothesis confirmed through experiments with copper sulfate and zinc sulfide...

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Related Experiment Video

Updated: Jul 6, 2026

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

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

Published on: September 17, 2017

Integrating diverse data for structure determination of macromolecular assemblies.

Frank Alber1, Friedrich Förster, Dmitry Korkin

  • 1Department of Biopharmaceutical Sciences, and California Institute for Quantitative Biosciences, University of California at San Francisco, CA 94158-2330, USA. alber@usc.edu

Annual Review of Biochemistry
|March 6, 2008
PubMed
Summary

Researchers developed a computational method to determine macromolecular assembly structures, like the nuclear pore complex (NPC), by integrating diverse experimental data for enhanced accuracy and efficiency.

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Combining Chemical Cross-linking and Mass Spectrometry of Intact Protein Complexes to Study the Architecture of Multi-subunit Protein Assemblies

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Related Experiment Videos

Last Updated: Jul 6, 2026

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

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

Published on: September 17, 2017

Structural Studies of Macromolecules in Solution using Small Angle X-Ray Scattering
07:19

Structural Studies of Macromolecules in Solution using Small Angle X-Ray Scattering

Published on: November 5, 2018

Combining Chemical Cross-linking and Mass Spectrometry of Intact Protein Complexes to Study the Architecture of Multi-subunit Protein Assemblies
10:01

Combining Chemical Cross-linking and Mass Spectrometry of Intact Protein Complexes to Study the Architecture of Multi-subunit Protein Assemblies

Published on: November 28, 2017

Area of Science:

  • Structural biology
  • Computational biology
  • Cell biology

Background:

  • Understanding cellular function requires knowledge of macromolecular assembly structures.
  • These assemblies can involve tens to hundreds of components.
  • Characterizing these structures requires integrating data at multiple resolution levels.

Purpose of the Study:

  • To develop a computational approach for determining macromolecular assembly structures.
  • To integrate diverse experimental data for improved structure determination.
  • To provide a framework for understanding biological organization from atoms to cells.

Main Methods:

  • Review of experimental data characterizing assemblies at various resolutions.
  • Description of computational methods for structure generation using experimental data.
  • Proposal of a hierarchical representation, scoring function with spatial restraints, and optimization method.

Main Results:

  • Demonstration of the computational approach using the yeast nuclear pore complex (NPC) with 456 proteins.
  • Generation of structures consistent with spatial information from experimental data.
  • Validation of the integrated computational strategy.

Conclusions:

  • The proposed computational approach enhances completeness, resolution, accuracy, and efficiency in structure determination.
  • This method enables the integration of structural information across biological scales.
  • The tools are poised to advance the understanding of complex cellular machinery.