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Related Concept Videos

Proteomics01:33

Proteomics

A proteome is the entire set of proteins that a cell type produces. We can study proteomes using the knowledge of genomes because genes code for mRNAs, and the mRNAs encode proteins. Although mRNA analysis is a step in the right direction, not all mRNAs are translated into proteins.
Proteomics is the study of proteomes' function. It involves the large-scale systematic study of the proteome to denote the protein complement expressed by a genome. Scientist Mark Wilkins coined the term proteomics...

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

Published on: November 5, 2018

NMR and small-angle scattering-based structural analysis of protein complexes in solution.

Tobias Madl1, Frank Gabel, Michael Sattler

  • 1Institute of Structural Biology, Helmholtz Zentrum München, Ingolstädter Landstr. 1, 85764 Neuherberg, Germany.

Journal of Structural Biology
|November 16, 2010
PubMed
Summary

Structural analysis of large protein complexes is advanced by combining solution Nuclear Magnetic Resonance (NMR) with Small-Angle Scattering (SAS) techniques. This integrated approach provides atomic-resolution insights into complex structures and dynamics.

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Analyzing Large Protein Complexes by Structural Mass Spectrometry
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Analyzing Large Protein Complexes by Structural Mass Spectrometry

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Last Updated: Jun 6, 2026

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

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

Analyzing Large Protein Complexes by Structural Mass Spectrometry
15:35

Analyzing Large Protein Complexes by Structural Mass Spectrometry

Published on: June 19, 2010

Area of Science:

  • Structural Biology
  • Biophysics
  • Molecular Biology

Background:

  • Analyzing multi-domain protein complexes is crucial for understanding cellular functions.
  • Solution-state techniques are vital for characterizing the dynamics and quaternary structure of these complexes.
  • Solution Nuclear Magnetic Resonance (NMR) offers atomic-resolution data but can be sparse for large complexes.

Purpose of the Study:

  • To review the utility and computational methods for integrating solution NMR with Small-Angle X-ray and Neutron Scattering (SAXS/SANS).
  • To discuss recent advancements in combining NMR and SAS for structural analysis of large protein complexes.
  • To illustrate the complementary nature of NMR and SAS for studying multi-domain proteins with flexible linkers.

Main Methods:

  • Integration of solution Nuclear Magnetic Resonance (NMR) data with Small-Angle X-ray Scattering (SAXS) and Small-Angle Neutron Scattering (SANS) data.
  • Application of computational approaches to combine sparse NMR data with SAS information.
  • Structural analysis of the tandem RNA recognition motif (RRM) domains of human splicing factor U2AF65 bound to a U9 RNA oligonucleotide.

Main Results:

  • Combining NMR and SAS provides a powerful strategy for structural determination of large and dynamic protein complexes.
  • Recent progress has enhanced the experimental and computational integration of these techniques.
  • The study illustrates the successful application to the U2AF65-U9 RNA complex, highlighting domain flexibility.

Conclusions:

  • Integrated NMR and SAS approaches are essential for comprehensive structural characterization of multi-domain proteins.
  • This combined methodology overcomes limitations of individual techniques, especially for large and flexible systems.
  • The findings provide atomic-level insights into the structural organization and dynamics of protein-RNA interactions.